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Iron in PDB 1cl6: Crystal Structures of Ferric-No Complexes of Fungal Nitric Oxide Reductase and Its SER286 Mutants at Cryogenic Temperature

Protein crystallography data

The structure of Crystal Structures of Ferric-No Complexes of Fungal Nitric Oxide Reductase and Its SER286 Mutants at Cryogenic Temperature, PDB code: 1cl6 was solved by S.-Y.Park, Y.Shiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.530, 81.710, 85.550, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 25.1

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structures of Ferric-No Complexes of Fungal Nitric Oxide Reductase and Its SER286 Mutants at Cryogenic Temperature (pdb code 1cl6). 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 Structures of Ferric-No Complexes of Fungal Nitric Oxide Reductase and Its SER286 Mutants at Cryogenic Temperature, PDB code: 1cl6:

Iron binding site 1 out of 1 in 1cl6

Go back to Iron Binding Sites List in 1cl6
Iron binding site 1 out of 1 in the Crystal Structures of Ferric-No Complexes of Fungal Nitric Oxide Reductase and Its SER286 Mutants at Cryogenic Temperature


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structures of Ferric-No Complexes of Fungal Nitric Oxide Reductase and Its SER286 Mutants at Cryogenic Temperature within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:9.3
occ:1.00
FE A:HEM501 0.0 9.3 1.0
N A:NO502 1.6 12.3 1.0
ND A:HEM501 2.0 8.9 1.0
NB A:HEM501 2.0 11.6 1.0
NA A:HEM501 2.0 8.4 1.0
NC A:HEM501 2.0 9.4 1.0
SG A:CYS352 2.3 11.3 1.0
O A:NO502 2.8 12.6 1.0
C4B A:HEM501 3.0 7.9 1.0
C1D A:HEM501 3.0 9.3 1.0
C4D A:HEM501 3.0 10.3 1.0
C1C A:HEM501 3.0 12.0 1.0
C1A A:HEM501 3.1 9.9 1.0
C4C A:HEM501 3.1 11.2 1.0
C1B A:HEM501 3.1 10.2 1.0
C4A A:HEM501 3.1 10.3 1.0
CHC A:HEM501 3.4 11.4 1.0
CHD A:HEM501 3.5 9.0 1.0
CHA A:HEM501 3.5 8.8 1.0
CHB A:HEM501 3.5 9.4 1.0
CB A:CYS352 3.5 8.0 1.0
C2D A:HEM501 4.3 8.6 1.0
C3B A:HEM501 4.3 12.0 1.0
CA A:CYS352 4.3 8.2 1.0
C3D A:HEM501 4.3 11.0 1.0
C2C A:HEM501 4.3 10.2 1.0
C2A A:HEM501 4.3 11.1 1.0
C2B A:HEM501 4.3 11.6 1.0
C3C A:HEM501 4.3 10.4 1.0
C3A A:HEM501 4.3 11.1 1.0
CA A:GLY240 4.6 11.3 1.0
O A:HOH576 4.9 16.5 1.0
O A:ALA239 4.9 13.7 1.0
N A:GLY240 4.9 11.8 1.0

Reference:

H.Shimizu, E.Obayashi, Y.Gomi, H.Arakawa, S.Y.Park, H.Nakamura, S.Adachi, H.Shoun, Y.Shiro. Proton Delivery in No Reduction By Fungal Nitric-Oxide Reductase. Cryogenic Crystallography, Spectroscopy, and Kinetics of Ferric-No Complexes of Wild-Type and Mutant Enzymes. J.Biol.Chem. V. 275 4816 2000.
ISSN: ISSN 0021-9258
PubMed: 10671516
DOI: 10.1074/JBC.275.7.4816
Page generated: Sun Dec 13 14:09:13 2020

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