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Iron in PDB 6qpx: Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii

Enzymatic activity of Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii

All present enzymatic activity of Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii:
1.7.2.1;

Protein crystallography data

The structure of Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii, PDB code: 6qpx was solved by S.V.Antonyuk, R.T.Shenoy, T.M.Hedison, R.R.Eady, S.S.Hasnain, N.S.Scrutton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.33 / 1.70
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 128.500, 128.500, 172.470, 90.00, 90.00, 120.00
R / Rfree (%) 17.4 / 20.3

Other elements in 6qpx:

The structure of Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii also contains other interesting chemical elements:

Copper (Cu) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii (pdb code 6qpx). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii, PDB code: 6qpx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 6qpx

Go back to Iron Binding Sites List in 6qpx
Iron binding site 1 out of 2 in the Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe503

b:14.8
occ:1.00
FE A:HEC503 0.0 14.8 1.0
ND A:HEC503 1.9 15.2 1.0
NA A:HEC503 2.0 15.1 1.0
NE2 A:HIS368 2.0 15.0 1.0
NB A:HEC503 2.0 14.8 1.0
NC A:HEC503 2.0 14.5 1.0
SD A:MET418 2.3 15.7 1.0
C1D A:HEC503 3.0 15.2 1.0
C4D A:HEC503 3.0 15.6 1.0
C1A A:HEC503 3.0 15.9 1.0
C4C A:HEC503 3.0 14.9 1.0
C4A A:HEC503 3.0 15.7 1.0
C4B A:HEC503 3.0 14.5 1.0
CE1 A:HIS368 3.0 15.8 1.0
C1B A:HEC503 3.0 14.8 1.0
CD2 A:HIS368 3.1 15.3 1.0
C1C A:HEC503 3.1 14.4 1.0
CE A:MET418 3.4 15.7 1.0
CG A:MET418 3.4 15.9 1.0
CHD A:HEC503 3.4 15.0 1.0
CHB A:HEC503 3.4 15.4 1.0
CHC A:HEC503 3.4 14.3 1.0
CHA A:HEC503 3.4 15.8 1.0
ND1 A:HIS368 4.1 16.1 1.0
CB A:MET418 4.2 16.5 1.0
CG A:HIS368 4.2 16.0 1.0
C2A A:HEC503 4.2 16.1 1.0
C3A A:HEC503 4.2 15.9 1.0
C2D A:HEC503 4.2 15.7 1.0
C3C A:HEC503 4.2 15.1 1.0
C3D A:HEC503 4.2 16.0 1.0
C2C A:HEC503 4.3 14.7 1.0
C2B A:HEC503 4.3 14.8 1.0
C3B A:HEC503 4.3 14.6 1.0

Iron binding site 2 out of 2 in 6qpx

Go back to Iron Binding Sites List in 6qpx
Iron binding site 2 out of 2 in the Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Nitrite Bound Y323A Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Fe503

b:13.4
occ:1.00
FE I:HEC503 0.0 13.4 1.0
ND I:HEC503 1.9 13.7 1.0
NA I:HEC503 2.0 13.6 1.0
NC I:HEC503 2.0 13.1 1.0
NB I:HEC503 2.0 13.6 1.0
NE2 I:HIS368 2.1 13.9 1.0
SD I:MET418 2.3 14.3 1.0
CE1 I:HIS368 3.0 14.5 1.0
C4D I:HEC503 3.0 14.1 1.0
C1D I:HEC503 3.0 13.7 1.0
C1A I:HEC503 3.0 14.2 1.0
C4C I:HEC503 3.0 13.5 1.0
C1B I:HEC503 3.0 13.7 1.0
C4B I:HEC503 3.0 13.4 1.0
C4A I:HEC503 3.0 14.0 1.0
C1C I:HEC503 3.0 13.2 1.0
CD2 I:HIS368 3.1 14.1 1.0
CHD I:HEC503 3.4 13.4 1.0
CHA I:HEC503 3.4 14.3 1.0
CE I:MET418 3.4 14.6 1.0
CHB I:HEC503 3.4 14.0 1.0
CHC I:HEC503 3.4 13.1 1.0
CG I:MET418 3.4 14.5 1.0
ND1 I:HIS368 4.1 14.8 1.0
CB I:MET418 4.2 15.1 1.0
C2A I:HEC503 4.2 14.4 1.0
C3C I:HEC503 4.2 13.6 1.0
CG I:HIS368 4.2 14.6 1.0
C2C I:HEC503 4.2 13.4 1.0
C3A I:HEC503 4.2 14.2 1.0
C2B I:HEC503 4.2 13.9 1.0
C3D I:HEC503 4.2 14.4 1.0
C2D I:HEC503 4.3 14.1 1.0
C3B I:HEC503 4.3 13.7 1.0

Reference:

T.M.Hedison, R.T.Shenoy, A.I.Iorgu, D.J.Heyes, K.Fisher, G.Wright, S.Hay, R.R.Eady, S.S.Hasnain, N.S.Scrutton. Unexpected Roles of A Tether Harboring A Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis Acs Catalysis 2019.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.9B01266
Page generated: Sun Dec 13 16:57:58 2020

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