Molybdenum in PDB 1n62: Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State

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

The structure of Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State, PDB code: 1n62 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)	17.80 / 1.09
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	117.860, 130.019, 156.231, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 17.2

The structure of Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State also contains other interesting chemical elements:

Iron	(Fe)	8 atoms
Copper	(Cu)	2 atoms

The binding sites of Molybdenum atom in the Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State (pdb code 1n62). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State, PDB code: 1n62:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ B:Mo3921 b:10.8 occ:1.00 MO B:CUB3921 0.0 10.8 1.0 OM1 B:CUB3921 1.7 10.4 1.0 OM2 B:CUB3921 2.0 12.7 1.0 S7' B:MCN3920 2.3 8.9 1.0 S B:CUB3921 2.4 11.6 0.9 S8' B:MCN3920 2.4 9.0 1.0 CZ B:CUB3921 2.6 12.9 1.0 C7' B:MCN3920 3.3 9.7 1.0 C8' B:MCN3920 3.3 9.4 1.0 OE2 B:GLU763 3.4 11.8 1.0 N B:GLY272 3.8 9.1 1.0 N B:GLY569 3.8 9.8 1.0 CA B:TYR568 3.9 10.3 1.0 NZ B:CUB3921 3.9 13.8 1.0 CA B:GLY272 3.9 10.3 1.0 O B:HOH3942 4.0 11.0 1.0 CB B:TYR568 4.0 10.6 1.0 CD B:GLU763 4.0 10.1 1.0 C B:PHE271 4.1 10.9 1.0 N B:ARG387 4.3 9.1 1.0 C B:TYR568 4.4 9.6 1.0 O B:PHE271 4.4 11.1 1.0 NE2 B:GLN240 4.5 10.0 1.0 CA B:ARG387 4.5 10.4 1.0 CG B:GLU763 4.5 9.8 1.0 C6' B:MCN3920 4.5 9.7 1.0 C1Z B:CUB3921 4.7 16.8 1.0 C9' B:MCN3920 4.7 9.6 1.0 CA B:PHE271 4.7 10.7 1.0 C2Z B:CUB3921 4.8 19.0 1.0 OE1 B:GLU763 4.8 11.2 1.0 CA B:GLY569 4.9 10.1 1.0 N5' B:MCN3920 5.0 9.2 1.0

Molybdenum binding site 2 out of 2 in the Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Crystal Structure of the Mo,Cu-Co Dehydrogenase (Codh), N- Butylisocyanide-Bound State within 5.0Å range: probe atom residue distance (Å) B Occ E:Mo4921 b:11.2 occ:1.00 MO E:CUB4921 0.0 11.2 1.0 OM1 E:CUB4921 1.7 10.9 1.0 OM2 E:CUB4921 2.0 12.5 1.0 S7' E:MCN4920 2.3 9.3 1.0 S E:CUB4921 2.4 12.1 0.9 S8' E:MCN4920 2.4 9.7 1.0 CZ E:CUB4921 2.7 13.1 1.0 C7' E:MCN4920 3.3 10.0 1.0 C8' E:MCN4920 3.3 9.8 1.0 OE2 E:GLU763 3.4 12.3 1.0 N E:GLY272 3.8 10.5 1.0 NZ E:CUB4921 3.9 15.3 1.0 N E:GLY569 3.9 9.9 1.0 CA E:GLY272 3.9 10.7 1.0 O E:HOH4929 3.9 11.7 1.0 CA E:TYR568 3.9 11.0 1.0 CB E:TYR568 4.0 11.1 1.0 CD E:GLU763 4.1 10.9 1.0 C E:PHE271 4.1 10.6 1.0 N E:ARG387 4.4 9.6 1.0 C E:TYR568 4.4 11.3 1.0 O E:PHE271 4.4 11.3 1.0 NE2 E:GLN240 4.5 11.2 1.0 CG E:GLU763 4.5 10.3 1.0 CA E:ARG387 4.5 9.8 1.0 C6' E:MCN4920 4.5 11.0 1.0 C1Z E:CUB4921 4.7 15.8 1.0 C9' E:MCN4920 4.7 10.2 1.0 CA E:PHE271 4.7 11.1 1.0 OE1 E:GLU763 4.9 11.5 1.0 CA E:GLY569 4.9 11.3 1.0 C2Z E:CUB4921 4.9 16.7 1.0 N5' E:MCN4920 4.9 9.4 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