Atomistry » Molybdenum » PDB 1aa6-1n61 » 1n60
Atomistry »
  Molybdenum »
    PDB 1aa6-1n61 »
      1n60 »

Molybdenum in PDB 1n60: Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form

Enzymatic activity of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form

All present enzymatic activity of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form:
1.2.99.2;

Protein crystallography data

The structure of Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form, PDB code: 1n60 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 / 1.19
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 118.566, 130.642, 158.492, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 17.1

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form (pdb code 1n60). 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 Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form, PDB code: 1n60:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1n60

Go back to Molybdenum Binding Sites List in 1n60
Molybdenum binding site 1 out of 2 in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form


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 Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mo4921

b:10.9
occ:1.00
MO B:OMO4921 0.0 10.9 1.0
OM1 B:OMO4921 1.7 10.4 1.0
OM2 B:OMO4921 1.8 12.3 1.0
OR1 B:OMO4921 1.8 11.4 1.0
S7' B:MCN4920 2.4 9.8 1.0
S8' B:MCN4920 2.5 9.5 1.0
C7' B:MCN4920 3.4 10.0 1.0
C8' B:MCN4920 3.4 9.8 1.0
OE2 B:GLU763 3.5 11.3 1.0
O B:HOH5764 3.6 19.2 1.0
N B:GLY272 3.8 10.7 1.0
CA B:GLY272 3.9 10.7 1.0
N B:GLY569 3.9 10.0 1.0
CA B:TYR568 3.9 10.6 1.0
CB B:TYR568 4.0 10.3 1.0
O B:HOH4968 4.1 11.0 1.0
CD B:GLU763 4.1 9.9 1.0
C B:PHE271 4.2 10.4 1.0
N B:ARG387 4.2 9.6 1.0
O B:HOH5346 4.4 25.8 1.0
C B:TYR568 4.4 9.9 1.0
CA B:ARG387 4.5 10.8 1.0
NE2 B:GLN240 4.5 10.7 1.0
O B:PHE271 4.6 10.7 1.0
CG B:GLU763 4.6 10.5 1.0
C6' B:MCN4920 4.7 9.7 1.0
CA B:PHE271 4.8 10.8 1.0
C9' B:MCN4920 4.8 9.4 1.0
OE1 B:GLU763 4.9 11.4 1.0
N B:TYR386 5.0 10.6 1.0
CA B:GLY569 5.0 10.2 1.0

Molybdenum binding site 2 out of 2 in 1n60

Go back to Molybdenum Binding Sites List in 1n60
Molybdenum binding site 2 out of 2 in the Crystal Structure of the Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form


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 Cu,Mo-Co Dehydrogenase (Codh); Cyanide- Inactivated Form within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mo5921

b:11.7
occ:1.00
MO E:OMO5921 0.0 11.7 1.0
OM1 E:OMO5921 1.7 11.8 1.0
OR1 E:OMO5921 1.8 12.0 1.0
OM2 E:OMO5921 1.8 13.0 1.0
S7' E:MCN5920 2.4 10.2 1.0
S8' E:MCN5920 2.5 10.3 1.0
C7' E:MCN5920 3.3 10.4 1.0
C8' E:MCN5920 3.4 10.4 1.0
OE2 E:GLU763 3.5 11.5 1.0
O E:HOH6732 3.7 20.7 1.0
N E:GLY272 3.8 10.9 1.0
CA E:GLY272 3.9 11.2 1.0
N E:GLY569 3.9 11.2 1.0
CA E:TYR568 4.0 11.3 1.0
O E:HOH5928 4.1 11.6 1.0
CB E:TYR568 4.1 11.6 1.0
CD E:GLU763 4.1 10.9 1.0
C E:PHE271 4.2 10.5 1.0
N E:ARG387 4.2 10.8 1.0
O E:HOH6317 4.3 24.1 1.0
C E:TYR568 4.5 11.3 1.0
CA E:ARG387 4.5 10.6 1.0
NE2 E:GLN240 4.5 11.3 1.0
O E:PHE271 4.5 11.5 1.0
CG E:GLU763 4.6 10.4 1.0
C6' E:MCN5920 4.7 10.6 1.0
CA E:PHE271 4.8 10.2 1.0
C9' E:MCN5920 4.9 11.1 1.0
N E:TYR386 4.9 10.8 1.0
OE1 E:GLU763 5.0 12.2 1.0
CA E:GLY569 5.0 11.3 1.0

Reference:

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
Page generated: Wed Sep 23 13:29:01 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy