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Molybdenum in PDB 1rm6: Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica

Enzymatic activity of Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica

All present enzymatic activity of Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica:
1.3.99.20;

Protein crystallography data

The structure of Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica, PDB code: 1rm6 was solved by M.Unciuleac, E.Warkentin, C.C.Page, P.L.Dutton, M.Boll, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.91 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 113.015, 151.845, 174.866, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 17.3

Other elements in 1rm6:

The structure of Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica also contains other interesting chemical elements:

Potassium (K) 1 atom
Iron (Fe) 24 atoms
Chlorine (Cl) 2 atoms
Sodium (Na) 2 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica (pdb code 1rm6). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica, PDB code: 1rm6:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1rm6

Go back to Molybdenum Binding Sites List in 1rm6
Molybdenum binding site 1 out of 2 in the Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo920

b:12.7
occ:1.00
MO A:PCD920 0.0 12.7 1.0
OM1 A:PCD920 1.7 13.0 1.0
OM2 A:PCD920 1.9 12.1 1.0
OR1 A:PCD920 2.1 13.2 1.0
S7' A:PCD920 2.3 11.2 1.0
S8' A:PCD920 2.4 10.6 1.0
C8' A:PCD920 3.3 8.3 1.0
C7' A:PCD920 3.3 10.8 1.0
O A:HOH9066 3.8 27.6 1.0
CA A:GLY246 3.9 9.2 1.0
OE2 A:GLU726 3.9 11.7 1.0
N A:GLY246 4.0 6.8 1.0
N A:SER522 4.1 12.1 1.0
C A:PHE245 4.2 9.1 1.0
CD A:GLU726 4.3 11.0 1.0
CA A:TYR521 4.3 10.8 1.0
O A:PHE245 4.4 9.9 1.0
NE2 A:GLN214 4.5 10.4 1.0
OE1 A:GLU726 4.5 12.1 1.0
CG2 A:THR249 4.5 9.4 1.0
O A:HOH6970 4.6 27.9 1.0
O A:SER520 4.7 12.3 1.0
C9' A:PCD920 4.7 8.8 1.0
C A:TYR521 4.7 9.9 1.0
C6' A:PCD920 4.7 8.6 1.0
N A:ARG358 4.8 11.8 1.0
CA A:ARG358 4.8 10.2 1.0
CA A:PHE245 5.0 7.6 1.0
CB A:TYR521 5.0 12.4 1.0
N5' A:PCD920 5.0 7.7 1.0

Molybdenum binding site 2 out of 2 in 1rm6

Go back to Molybdenum Binding Sites List in 1rm6
Molybdenum binding site 2 out of 2 in the Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Structure of 4-Hydroxybenzoyl-Coa Reductase From Thauera Aromatica within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mo920

b:11.1
occ:1.00
MO D:PCD920 0.0 11.1 1.0
OM1 D:PCD920 1.6 10.7 1.0
OM2 D:PCD920 1.9 12.7 1.0
OR1 D:PCD920 2.1 10.8 1.0
S7' D:PCD920 2.3 9.5 1.0
S8' D:PCD920 2.4 8.8 1.0
C7' D:PCD920 3.3 10.5 1.0
C8' D:PCD920 3.3 7.4 1.0
O D:HOH6522 3.9 27.4 1.0
OE2 D:GLU726 3.9 12.1 1.0
CA D:GLY246 4.0 6.9 1.0
N D:GLY246 4.0 7.1 1.0
N D:SER522 4.1 7.8 1.0
C D:PHE245 4.2 6.7 1.0
CD D:GLU726 4.3 13.3 1.0
CA D:TYR521 4.3 12.3 1.0
O D:PHE245 4.4 8.8 1.0
NE2 D:GLN214 4.4 8.5 1.0
OE1 D:GLU726 4.5 11.7 1.0
O D:HOH6476 4.5 25.7 1.0
CG2 D:THR249 4.6 8.8 1.0
O D:SER520 4.6 12.0 1.0
C D:TYR521 4.7 12.9 1.0
C9' D:PCD920 4.7 8.0 1.0
C6' D:PCD920 4.7 8.2 1.0
N D:ARG358 4.8 9.4 1.0
CA D:ARG358 4.8 11.1 1.0
CA D:PHE245 5.0 7.1 1.0
N5' D:PCD920 5.0 7.2 1.0
CB D:TYR521 5.0 12.8 1.0

Reference:

M.Unciuleac, E.Warkentin, C.C.Page, M.Boll, U.Ermler. Structure of A Xanthine Oxidase-Related 4-Hydroxybenzoyl-Coa Reductase with An Additional [4FE-4S] Cluster and An Inverted Electron Flow Structure V. 12 2249 2004.
ISSN: ISSN 0969-2126
PubMed: 15576037
DOI: 10.1016/J.STR.2004.10.008
Page generated: Tue Dec 15 05:16:31 2020

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