Copper in PDB 1n61: Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State

All present enzymatic activity of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State:
1.2.99.2;

The structure of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State, PDB code: 1n61 was solved by H.Dobbek, L.Gremer, R.Kiefersauer, R.Huber, O.Meyer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.00 / 1.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	119.162, 131.375, 160.318, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 18.4

The structure of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Iron	(Fe)	8 atoms

The binding sites of Copper atom in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State (pdb code 1n61). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State, PDB code: 1n61:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu3921 b:11.9 occ:0.90 CU B:CUN3921 0.0 11.9 0.9 S B:CUN3921 2.1 9.3 1.0 SG B:CYS388 2.2 9.8 1.0 O B:HOH4307 2.7 24.3 1.0 N B:CYS388 3.1 8.8 1.0 CB B:CYS388 3.2 9.8 1.0 OM2 B:CUN3921 3.3 11.4 1.0 N B:ALA385 3.4 9.3 1.0 CA B:CYS388 3.5 10.3 1.0 N B:SER389 3.5 9.8 1.0 C B:ALA385 3.6 9.0 1.0 CA B:ALA385 3.6 9.4 1.0 O B:ALA385 3.6 9.7 1.0 CG1 B:VAL384 3.8 12.3 1.0 OE2 B:GLU763 3.8 10.5 1.0 C B:CYS388 3.9 9.1 1.0 MO B:CUN3921 3.9 9.6 1.0 C B:VAL384 3.9 10.0 1.0 N B:PHE390 4.1 9.5 1.0 N B:ARG387 4.2 8.8 1.0 N B:TYR386 4.2 9.5 1.0 C B:ARG387 4.2 8.2 1.0 O B:HOH4410 4.4 32.0 1.0 CA B:VAL384 4.5 11.1 1.0 CA B:ARG387 4.5 10.0 1.0 CA B:SER389 4.5 9.9 1.0 O B:VAL384 4.7 11.7 1.0 CB B:VAL384 4.7 12.8 1.0 C B:TYR386 4.7 9.9 1.0 C B:SER389 4.9 9.6 1.0 O B:CYS388 4.9 9.6 1.0 OM1 B:CUN3921 5.0 9.6 1.0

Copper binding site 2 out of 2 in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Dithionite Reduced State within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu4921 b:12.5 occ:0.90 CU E:CUN4921 0.0 12.5 0.9 SG E:CYS388 2.2 10.2 1.0 S E:CUN4921 2.2 10.4 1.0 O E:HOH5292 2.7 27.2 1.0 N E:CYS388 3.1 10.0 1.0 CB E:CYS388 3.2 10.7 1.0 N E:ALA385 3.3 10.2 1.0 OM2 E:CUN4921 3.4 13.7 1.0 CA E:CYS388 3.5 9.4 1.0 C E:ALA385 3.5 10.4 1.0 N E:SER389 3.6 10.8 1.0 CA E:ALA385 3.6 10.7 1.0 O E:ALA385 3.7 9.8 1.0 OE2 E:GLU763 3.8 10.6 1.0 CG1 E:VAL384 3.8 12.9 1.0 C E:CYS388 3.9 9.7 1.0 MO E:CUN4921 3.9 10.6 1.0 C E:VAL384 4.0 11.9 1.0 N E:PHE390 4.2 9.9 1.0 N E:ARG387 4.2 9.6 1.0 N E:TYR386 4.2 9.2 1.0 C E:ARG387 4.2 9.3 1.0 CA E:VAL384 4.5 11.3 1.0 CA E:ARG387 4.5 8.1 1.0 CA E:SER389 4.6 10.0 1.0 O E:HOH5773 4.6 30.6 1.0 O E:VAL384 4.6 12.5 1.0 C E:TYR386 4.8 8.8 1.0 CB E:VAL384 4.8 11.8 1.0 C E:SER389 4.9 9.7 1.0 O E:CYS388 4.9 10.3 1.0

H.Dobbek, L.Gremer, R.Kiefersauer, R.Huber, O.Meyer. Catalysis at A Dinuclear [Cusmo(=O)Oh] Cluster in A Co Dehydrogenase Resolved at 1.1-A Resolution Proc.Natl.Acad.Sci.Usa V. 99 15971 2002.
ISSN: ISSN 0027-8424
PubMed: 12475995
DOI: 10.1073/PNAS.212640899