Atomistry » Platinum » PDB 3co3-3wu9 » 3tur
Atomistry »
  Platinum »
    PDB 3co3-3wu9 »
      3tur »

Platinum in PDB 3tur: Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment

Protein crystallography data

The structure of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment, PDB code: 3tur was solved by M.A.Bianchet, S.B.Erdemli, R.Gupta, G.Lamichhane, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 85.69 / 1.72
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 119.132, 120.829, 122.847, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 23.5

Other elements in 3tur:

The structure of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment also contains other interesting chemical elements:

Iodine (I) 11 atoms

Platinum Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Platinum atom in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment (pdb code 3tur). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total 12 binding sites of Platinum where determined in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment, PDB code: 3tur:
Jump to Platinum binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Platinum binding site 1 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 1 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt501

b:49.9
occ:0.30
PT1 A:0JC501 0.0 49.9 0.3
N2 A:0JC501 2.0 52.5 0.3
N1 A:0JC501 2.0 55.7 0.3
I1 A:0JC501 2.4 59.3 0.3
ND1 A:HIS347 2.7 48.6 1.0
C2 A:0JC501 2.7 52.8 0.3
C1 A:0JC501 2.9 56.1 0.3
CB A:HIS347 3.2 31.7 1.0
CG A:HIS347 3.3 40.3 1.0
CA A:HIS347 3.3 30.4 1.0
O A:HIS347 3.8 30.4 1.0
CE1 A:HIS347 3.9 50.1 1.0
C A:HIS347 4.0 30.4 1.0
O A:GLY346 4.1 32.3 1.0
N A:HIS347 4.5 29.7 1.0
CD2 A:HIS347 4.6 44.9 1.0
C A:GLY346 4.7 31.5 1.0
NE2 A:HIS347 4.8 47.4 1.0

Platinum binding site 2 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 2 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 2 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt502

b:0.8
occ:0.50
PT1 A:0JC502 0.0 0.8 0.5
SD A:MET157 0.7 63.9 0.5
N1 A:0JC502 2.0 1.0 0.5
N2 A:0JC502 2.1 0.8 0.5
CE A:MET157 2.2 58.4 0.5
PT1 A:0JC502 2.3 54.6 0.5
CG A:MET157 2.3 42.7 0.5
SD A:MET157 2.4 85.5 0.5
I1 A:0JC502 2.7 0.1 0.5
C1 A:0JC502 2.7 0.7 0.5
C2 A:0JC502 2.9 0.9 0.5
CB A:MET157 3.1 39.8 0.5
CB A:MET157 3.1 33.1 0.5
N2 A:0JC502 3.2 61.4 0.5
CG A:MET157 3.3 57.2 0.5
I1 A:0JC502 3.5 88.5 0.5
CE A:MET157 3.6 84.1 0.5
N1 A:0JC502 4.3 59.9 0.5
C2 A:0JC502 4.4 57.6 0.5
CA A:MET157 4.5 32.8 0.5
CA A:MET157 4.6 36.9 0.5
N A:MET157 4.9 32.6 0.5
N A:MET157 5.0 35.1 0.5

Platinum binding site 3 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 3 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 3 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt502

b:54.6
occ:0.50
PT1 A:0JC502 0.0 54.6 0.5
I1 A:0JC502 1.8 0.1 0.5
N2 A:0JC502 2.1 61.4 0.5
N1 A:0JC502 2.1 59.9 0.5
SD A:MET157 2.3 85.5 0.5
PT1 A:0JC502 2.3 0.8 0.5
SD A:MET157 2.5 63.9 0.5
I1 A:0JC502 2.7 88.5 0.5
C2 A:0JC502 2.9 57.6 0.5
C1 A:0JC502 3.0 57.7 0.5
CG A:MET157 3.3 57.2 0.5
CE A:MET157 3.7 58.4 0.5
CG A:MET157 3.7 42.7 0.5
N1 A:0JC502 3.8 1.0 0.5
CB A:MET157 3.8 33.1 0.5
CB A:MET157 3.9 39.8 0.5
O A:HOH737 4.0 35.1 1.0
CE A:MET157 4.0 84.1 0.5
N2 A:0JC502 4.1 0.8 0.5
OH A:TYR330 4.3 55.8 1.0
OE2 A:GLU168 4.6 37.8 1.0
NE A:ARG371 4.9 67.0 1.0
C1 A:0JC502 4.9 0.7 0.5

Platinum binding site 4 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 4 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 4 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt503

b:69.4
occ:0.30
PT1 A:0JC503 0.0 69.4 0.3
N1 A:0JC503 2.0 71.9 0.3
N2 A:0JC503 2.1 72.4 0.3
SD A:MET237 2.3 79.3 1.0
I1 A:0JC503 2.5 78.8 0.3
C1 A:0JC503 2.8 70.9 0.3
C2 A:0JC503 2.9 70.5 0.3
CG A:MET237 3.3 62.8 1.0
CE A:MET237 3.3 65.8 1.0
CA A:HIS150 4.4 54.8 1.0
CB A:MET237 4.8 55.8 1.0
CB A:HIS150 5.0 55.9 1.0

Platinum binding site 5 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 5 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 5 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt504

b:0.4
occ:0.50
PT1 A:0JC504 0.0 0.4 0.5
PT1 A:0JC504 0.6 0.0 0.5
N2 A:0JC504 1.9 0.6 0.5
N1 A:0JC504 2.0 0.7 0.5
N1 A:0JC504 2.1 99.0 0.5
N2 A:0JC504 2.1 97.6 0.5
ND1 A:HIS214 2.2 87.1 1.0
I1 A:0JC504 2.7 0.3 0.5
C2 A:0JC504 2.7 0.5 0.5
C1 A:0JC504 2.9 0.0 0.5
C2 A:0JC504 3.0 96.2 0.5
C1 A:0JC504 3.1 95.8 0.5
I1 A:0JC504 3.1 0.8 0.5
CG A:HIS214 3.2 62.4 1.0
CE1 A:HIS214 3.2 79.5 1.0
CA A:HIS214 3.3 37.9 1.0
CB A:HIS214 3.4 41.9 1.0
N A:PHE215 3.8 33.2 1.0
O A:GLU213 4.1 38.1 1.0
C A:HIS214 4.1 34.8 1.0
CD2 A:HIS214 4.3 63.7 1.0
NE2 A:HIS214 4.3 67.2 1.0
N A:HIS214 4.4 35.1 1.0
C A:GLU213 4.6 35.7 1.0
CG A:PHE215 4.8 28.4 1.0
CD1 A:PHE215 4.9 31.0 1.0
CD2 A:PHE215 4.9 31.5 1.0

Platinum binding site 6 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 6 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 6 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt504

b:0.0
occ:0.50
PT1 A:0JC504 0.0 0.0 0.5
PT1 A:0JC504 0.6 0.4 0.5
N2 A:0JC504 1.8 97.6 0.5
N1 A:0JC504 2.1 0.7 0.5
N2 A:0JC504 2.1 0.6 0.5
N1 A:0JC504 2.1 99.0 0.5
ND1 A:HIS214 2.2 87.1 1.0
C2 A:0JC504 2.6 96.2 0.5
I1 A:0JC504 2.7 0.8 0.5
C1 A:0JC504 2.9 95.8 0.5
CE1 A:HIS214 3.0 79.5 1.0
C2 A:0JC504 3.0 0.5 0.5
C1 A:0JC504 3.1 0.0 0.5
I1 A:0JC504 3.1 0.3 0.5
CG A:HIS214 3.4 62.4 1.0
CA A:HIS214 3.8 37.9 1.0
CB A:HIS214 3.9 41.9 1.0
O A:GLU213 4.2 38.1 1.0
NE2 A:HIS214 4.3 67.2 1.0
N A:PHE215 4.4 33.2 1.0
CD2 A:HIS214 4.4 63.7 1.0
C A:HIS214 4.7 34.8 1.0
N A:HIS214 4.8 35.1 1.0
C A:GLU213 4.9 35.7 1.0

Platinum binding site 7 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 7 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 7 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pt501

b:82.4
occ:0.50
SD B:MET237 2.3 79.1 0.8
CE B:MET237 3.1 78.9 1.0
CG B:MET237 3.4 67.1 1.0
N B:HIS150 3.8 65.0 1.0
OE1 B:GLU176 4.7 69.3 1.0
CB B:MET237 4.8 59.2 1.0
CA B:HIS150 4.8 64.0 1.0
O B:GLU235 4.9 60.9 1.0
O B:GLY236 5.0 59.0 1.0

Platinum binding site 8 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 8 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 8 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pt502

b:61.9
occ:0.60
PT1 B:0JC502 0.0 61.9 0.6
N2 B:0JC502 2.1 66.5 0.6
N1 B:0JC502 2.1 68.2 0.6
ND1 B:HIS347 2.1 50.5 1.0
I1 B:0JC502 2.6 85.1 0.6
C2 B:0JC502 2.8 65.9 0.6
C1 B:0JC502 2.9 66.3 0.6
CE1 B:HIS347 3.1 48.9 1.0
CG B:HIS347 3.2 37.9 1.0
CB B:HIS347 3.5 33.0 1.0
CA B:HIS347 3.7 31.5 1.0
O B:HOH718 3.8 77.8 1.0
O B:GLY346 4.0 32.7 1.0
NE2 B:HIS347 4.2 45.4 1.0
CD2 B:HIS347 4.3 42.4 1.0
O B:HIS347 4.6 30.7 1.0
C B:HIS347 4.7 30.7 1.0
N B:HIS347 4.7 29.1 1.0
C B:GLY346 4.8 30.4 1.0

Platinum binding site 9 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 9 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 9 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pt503

b:0.6
occ:0.30
PT1 B:0JC503 0.0 0.6 0.3
N2 B:0JC503 2.0 0.4 0.3
N1 B:0JC503 2.0 0.3 0.3
I1 B:0JC503 2.6 0.5 1.0
C2 B:0JC503 2.8 0.0 0.3
C1 B:0JC503 2.8 0.1 0.3
ND1 B:HIS214 3.2 48.2 1.0
O B:GLU213 3.7 37.5 1.0
CA B:HIS214 3.9 35.9 1.0
CG B:HIS214 4.1 45.1 1.0
CE1 B:HIS214 4.1 53.8 1.0
CB B:HIS214 4.2 37.6 1.0
N B:PHE215 4.4 33.2 1.0
C B:GLU213 4.6 36.5 1.0
C B:HIS214 4.6 33.7 1.0
N B:HIS214 4.7 35.7 1.0
CE3 B:TRP394 4.8 32.0 1.0
O B:HOH624 4.8 73.5 1.0
CZ3 B:TRP394 4.9 33.3 1.0

Platinum binding site 10 out of 12 in 3tur

Go back to Platinum Binding Sites List in 3tur
Platinum binding site 10 out of 12 in the Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 10 of Crystal Structure of M. Tuberculosis Ld-Transpeptidase Type 2 Complexed with A Peptidoglycan Fragment within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pt504

b:13.9
occ:0.10
PT1 B:0JC504 0.0 13.9 0.1
N2 B:0JC504 0.7 14.4 0.5
PT1 B:0JC504 1.3 63.0 0.5
N1 B:0JC504 2.0 41.9 0.1
N2 B:0JC504 2.0 34.3 0.1
C2 B:0JC504 2.1 45.0 0.5
SD B:MET157 2.3 57.0 1.0
I1 B:0JC504 2.6 28.5 0.1
N1 B:0JC504 2.7 67.8 0.5
C1 B:0JC504 2.8 40.1 0.1
C1 B:0JC504 2.9 35.5 0.5
C2 B:0JC504 2.9 45.0 0.1
CE B:MET157 3.7 54.4 1.0
O B:HOH782 3.7 74.8 1.0
CG B:MET157 3.8 47.2 1.0
I1 B:0JC504 3.9 83.8 0.5
O B:HOH841 4.0 38.2 1.0
CB B:MET157 4.1 34.9 1.0
CD B:ARG371 4.1 51.8 1.0
OE2 B:GLU168 4.3 36.2 1.0
O B:HOH623 4.4 39.1 1.0
NE B:ARG371 4.4 58.0 1.0
OH B:TYR330 4.6 59.7 1.0
O B:HOH838 4.7 0.8 1.0
CZ B:ARG371 4.8 55.2 1.0
NH2 B:ARG371 4.8 49.9 1.0

Reference:

S.B.Erdemli, R.Gupta, W.R.Bishai, G.Lamichhane, L.M.Amzel, M.A.Bianchet. Targeting the Cell Wall of Mycobacterium Tuberculosis: Structure and Mechanism of L,D-Transpeptidase 2. Structure V. 20 2103 2012.
ISSN: ISSN 0969-2126
PubMed: 23103390
DOI: 10.1016/J.STR.2012.09.016
Page generated: Wed Dec 16 02:04:28 2020

Last articles

Tb in 6TVY
Si in 6Y7O
Rh in 6WRM
Rh in 6WRL
Ni in 6Y8Z
Ni in 6Y8Y
Na in 6ZXZ
Na in 7ACG
Na in 6YLS
Na in 6Y8Z
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy