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Platinum in PDB 6zlx: The Structure of the Clpx-Associated Factor PDIP38

Protein crystallography data

The structure of The Structure of the Clpx-Associated Factor PDIP38, PDB code: 6zlx was solved by K.Zeth, D.Dougan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.31 / 3.39
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 120.095, 120.095, 48.586, 90, 90, 120
R / Rfree (%) 24.7 / 28.7

Platinum Binding Sites:

The binding sites of Platinum atom in the The Structure of the Clpx-Associated Factor PDIP38 (pdb code 6zlx). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total 2 binding sites of Platinum where determined in the The Structure of the Clpx-Associated Factor PDIP38, PDB code: 6zlx:
Jump to Platinum binding site number: 1; 2;

Platinum binding site 1 out of 2 in 6zlx

Go back to Platinum Binding Sites List in 6zlx
Platinum binding site 1 out of 2 in the The Structure of the Clpx-Associated Factor PDIP38


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of The Structure of the Clpx-Associated Factor PDIP38 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt401

b:192.9
occ:1.00
CE A:MET249 2.8 239.3 1.0
CE1 A:HIS319 2.8 151.7 1.0
ND1 A:HIS319 2.9 139.6 1.0
CB A:MET249 3.6 204.3 1.0
CG A:MET249 3.8 227.8 1.0
CB A:ARG263 3.8 97.0 1.0
SD A:MET249 4.0 251.3 1.0
NE2 A:HIS319 4.1 148.9 1.0
CG A:HIS319 4.3 140.3 1.0
CD1 A:TRP261 4.4 165.1 1.0
O A:TRP262 4.7 132.4 1.0
NE1 A:TRP261 4.7 157.6 1.0
C A:TRP262 4.8 122.6 1.0
CA A:ARG263 4.8 110.8 1.0
N A:ARG263 4.8 117.6 1.0
CA A:MET249 4.9 184.4 1.0
CD2 A:HIS319 4.9 147.4 1.0
O A:MET249 5.0 208.2 1.0

Platinum binding site 2 out of 2 in 6zlx

Go back to Platinum Binding Sites List in 6zlx
Platinum binding site 2 out of 2 in the The Structure of the Clpx-Associated Factor PDIP38


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 2 of The Structure of the Clpx-Associated Factor PDIP38 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt402

b:284.1
occ:1.00
SG A:CYS265 2.7 132.3 1.0
CB A:CYS265 2.9 99.5 1.0
OD1 A:ASP173 3.6 125.8 1.0
NE2 A:GLN315 3.9 123.5 1.0
CA A:CYS265 4.1 90.8 1.0
CG A:ASP173 4.1 128.4 1.0
OD2 A:ASP173 4.2 152.7 1.0
CD A:GLN315 4.4 114.4 1.0
O A:TYR316 4.4 104.2 1.0
CB A:SER317 4.4 115.0 1.0
CG A:GLN315 4.6 113.9 1.0
C A:CYS265 4.9 124.9 1.0
OG A:SER317 5.0 109.5 1.0

Reference:

P.Strack, E.Brodie, H.Zhan, V.Schuenemann, T.Saiyed, K.Zeth, K.Truscott, D.Dougan. PDIP38 Is A Novel Adaptor-Like Modulator of the Mitochondrial Aaa+ Protease Clpxp To Be Published.
Page generated: Sat Aug 21 17:32:15 2021

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