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Manganese in PDB 7qbp: Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea

Protein crystallography data

The structure of Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea, PDB code: 7qbp was solved by V.Srinivas, R.Diamanti, H.Lebrette, M.Hogbom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.05 / 1.38
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 103.173, 103.173, 61.574, 90, 90, 90
R / Rfree (%) 15.2 / 16.5

Other elements in 7qbp:

The structure of Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea also contains other interesting chemical elements:

Iron (Fe) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea (pdb code 7qbp). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea, PDB code: 7qbp:

Manganese binding site 1 out of 1 in 7qbp

Go back to Manganese Binding Sites List in 7qbp
Manganese binding site 1 out of 1 in the Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:17.2
occ:1.00
OE1 A:GLU73 2.0 19.8 1.0
O1 A:PLM403 2.0 25.0 1.0
OE1 A:GLU106 2.1 17.4 1.0
O A:HOH544 2.1 20.1 1.0
ND1 A:HIS109 2.2 15.8 1.0
O A:HOH502 2.4 30.9 1.0
C1 A:PLM403 2.9 22.4 1.0
CD A:GLU73 3.0 19.7 1.0
CD A:GLU106 3.1 15.2 1.0
CE1 A:HIS109 3.1 16.4 1.0
HE1 A:HIS109 3.1 19.7 1.0
O2 A:PLM403 3.2 23.5 1.0
OE2 A:GLU73 3.2 22.0 1.0
CG A:HIS109 3.3 14.9 1.0
OE2 A:GLU106 3.4 18.1 1.0
FE A:FE402 3.4 18.1 1.0
HB2 A:HIS109 3.5 17.6 1.0
HB3 A:HIS109 3.7 17.6 1.0
HA A:GLU106 3.7 16.9 1.0
CB A:HIS109 3.8 14.7 1.0
HE1 A:HIS210 4.0 19.6 1.0
OE2 A:GLU207 4.0 27.5 1.0
HG23 A:VAL76 4.1 18.2 1.0
HA A:GLU73 4.2 18.6 1.0
NE2 A:HIS109 4.2 16.1 1.0
C2 A:PLM403 4.3 25.4 1.0
CG A:GLU73 4.3 17.2 1.0
H31 A:PLM403 4.3 30.2 1.0
CD2 A:HIS109 4.4 15.9 1.0
CG A:GLU106 4.4 15.3 1.0
HB3 A:GLU73 4.4 19.5 1.0
HB A:ILE203 4.5 21.2 1.0
H32 A:PLM403 4.6 30.2 1.0
HB3 A:GLU106 4.6 17.3 1.0
OE1 A:GLU207 4.6 20.6 1.0
CA A:GLU106 4.6 14.1 1.0
C3 A:PLM403 4.7 25.2 1.0
CE1 A:HIS210 4.7 16.4 1.0
H21 A:PLM403 4.7 30.4 1.0
CD A:GLU207 4.7 24.8 1.0
HG22 A:VAL76 4.7 18.2 1.0
CB A:GLU73 4.7 16.2 1.0
CB A:GLU106 4.8 14.4 1.0
ND1 A:HIS210 4.8 16.8 1.0
HG3 A:GLU73 4.8 20.6 1.0
CG2 A:VAL76 4.8 15.2 1.0
HG2 A:GLU73 4.9 20.6 1.0
HG2 A:GLU106 4.9 18.4 1.0
OH A:TYR180 4.9 22.0 1.0
HH A:TYR180 4.9 26.4 1.0
CA A:GLU73 4.9 15.5 1.0
HG3 A:GLU106 5.0 18.4 1.0
HG21 A:VAL76 5.0 18.2 1.0
HE2 A:HIS109 5.0 19.3 1.0

Reference:

R.Diamanti, V.Srinivas, A.I.Johansson, A.Nordstrom, J.J.Griese, H.Lebrette, M.Hogbom. Comparative Structural Analysis Provides New Insights Into the Function of R2-Like Ligand-Binding Oxidase. Febs Lett. V. 596 1600 2022.
ISSN: ISSN 0014-5793
PubMed: 35175627
DOI: 10.1002/1873-3468.14319
Page generated: Sun Oct 6 10:25:52 2024

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