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Platinum in PDB 3ro1: Crystal Structure of the Complex of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Terpyridine Platinum(II)

Enzymatic activity of Crystal Structure of the Complex of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Terpyridine Platinum(II)

All present enzymatic activity of Crystal Structure of the Complex of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Terpyridine Platinum(II):
3.1.3.48;

Protein crystallography data

The structure of Crystal Structure of the Complex of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Terpyridine Platinum(II), PDB code: 3ro1 was solved by Y.-C.Lo, A.H.-J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.90
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 72.756, 72.756, 32.302, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 24.2

Platinum Binding Sites:

The binding sites of Platinum atom in the Crystal Structure of the Complex of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Terpyridine Platinum(II) (pdb code 3ro1). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total only one binding site of Platinum was determined in the Crystal Structure of the Complex of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Terpyridine Platinum(II), PDB code: 3ro1:

Platinum binding site 1 out of 1 in 3ro1

Go back to Platinum Binding Sites List in 3ro1
Platinum binding site 1 out of 1 in the Crystal Structure of the Complex of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Terpyridine Platinum(II)


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 the Complex of the Archaeal Sulfolobus Ptp-Fold Phosphatase with Terpyridine Platinum(II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt165

b:72.2
occ:1.00
PT1 A:TPT165 0.0 72.2 1.0
N2 A:TPT165 2.0 63.2 1.0
N3 A:TPT165 2.0 61.8 1.0
N1 A:TPT165 2.1 63.6 1.0
O A:HOH281 2.2 33.8 1.0
C11 A:TPT165 2.9 62.1 1.0
C10 A:TPT165 2.9 62.7 1.0
C5 A:TPT165 2.9 64.0 1.0
C6 A:TPT165 2.9 64.2 1.0
C15 A:TPT165 3.0 62.5 1.0
C1 A:TPT165 3.0 64.6 1.0
CD2 A:TRP39 3.7 27.4 1.0
CE2 A:TRP39 3.7 28.8 1.0
CE3 A:TRP39 3.8 27.0 1.0
CZ2 A:TRP39 3.8 29.6 1.0
CZ3 A:TRP39 3.8 29.9 1.0
CH2 A:TRP39 3.9 28.9 1.0
C12 A:TPT165 4.2 62.2 1.0
C9 A:TPT165 4.2 62.7 1.0
C7 A:TPT165 4.3 63.5 1.0
C4 A:TPT165 4.3 64.0 1.0
C14 A:TPT165 4.3 62.4 1.0
C2 A:TPT165 4.4 64.1 1.0
NE1 A:TRP39 4.4 28.2 1.0
CG A:TRP39 4.4 25.5 1.0
CD1 A:TRP39 4.7 27.2 1.0
C8 A:TPT165 4.8 63.3 1.0
C13 A:TPT165 4.8 62.4 1.0
C3 A:TPT165 4.9 64.3 1.0

Reference:

Y.-C.Lo, W.-C.Su, T.-P.Ko, N.-C.Wang, A.H.-J.Wang. Terpyridine Platinum(II) Complexes Inhibit Cysteine Proteases By Binding to Active-Site Cysteine. J.Biomol.Struct.Dyn. V. 29 267 2011.
ISSN: ESSN 1538-0254
PubMed: 21875148
DOI: 10.1080/073911011010524993
Page generated: Wed Dec 16 02:04:28 2020

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