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Iron in PDB 7qq2: Crystal Structure of As-Isolated S321M Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

Enzymatic activity of Crystal Structure of As-Isolated S321M Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

All present enzymatic activity of Crystal Structure of As-Isolated S321M Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii:
1.7.2.1;

Protein crystallography data

The structure of Crystal Structure of As-Isolated S321M Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 7qq2 was solved by N.Petchyam, S.Antonyuk, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 73.65 / 2.10
Space group I 21 3
Cell size a, b, c (Å), α, β, γ (°) 180.14, 180.14, 180.14, 90, 90, 90
R / Rfree (%) 15.3 / 18.6

Other elements in 7qq2:

The structure of Crystal Structure of As-Isolated S321M Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of As-Isolated S321M Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii (pdb code 7qq2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of As-Isolated S321M Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 7qq2:

Iron binding site 1 out of 1 in 7qq2

Go back to Iron Binding Sites List in 7qq2
Iron binding site 1 out of 1 in the Crystal Structure of As-Isolated S321M Mutant of Three-Domain Heme-Cu 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 As-Isolated S321M Mutant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe503

b:38.3
occ:1.00
 FE A:HEC503 0.0 38.3 1.0
NE2 A:HIS368 1.9 36.0 1.0
ND A:HEC503 2.1 46.8 1.0
NC A:HEC503 2.1 39.5 1.0
NB A:HEC503 2.1 43.3 1.0
NA A:HEC503 2.1 47.3 1.0
SD A:MET418 2.2 37.0 1.0
CE1 A:HIS368 2.9 39.7 1.0
CD2 A:HIS368 3.0 38.2 1.0
C1C A:HEC503 3.1 35.6 1.0
C4B A:HEC503 3.1 40.4 1.0
C4D A:HEC503 3.1 41.8 1.0
C1D A:HEC503 3.1 42.7 1.0
C4C A:HEC503 3.1 36.8 1.0
C1A A:HEC503 3.1 41.8 1.0
C1B A:HEC503 3.1 44.1 1.0
C4A A:HEC503 3.1 43.8 1.0
CG A:MET418 3.3 39.7 1.0
CE A:MET418 3.4 38.7 1.0
CHA A:HEC503 3.4 42.0 1.0
CHC A:HEC503 3.4 36.1 1.0
CHD A:HEC503 3.4 35.4 1.0
CHB A:HEC503 3.5 39.7 1.0
ND1 A:HIS368 4.0 36.2 1.0
CG A:HIS368 4.1 33.7 1.0
CB A:MET418 4.2 41.3 1.0
C3B A:HEC503 4.4 39.1 1.0
C3D A:HEC503 4.4 43.8 1.0
C3C A:HEC503 4.4 35.2 1.0
C2D A:HEC503 4.4 43.3 1.0
C2C A:HEC503 4.4 37.5 1.0
C2A A:HEC503 4.4 46.7 1.0
C2B A:HEC503 4.4 40.1 1.0
C3A A:HEC503 4.4 47.5 1.0

Reference:

N.Petchyam, S.Antonyuk, S.S.Hasnain. Structural Studies of Haem Three-Domain Copper Nitrite Reductase Mutants From Ralstonia Pickettii To Be Published.
Page generated: Thu Aug 8 19:52:47 2024

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