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Iron in PDB 1d3s: 1.4 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixis at pH=5.6.

Protein crystallography data

The structure of 1.4 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixis at pH=5.6., PDB code: 1d3s was solved by A.Weichsel, J.F.Andersen, S.A.Roberts, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.180, 42.520, 52.860, 90.00, 94.35, 90.00
R / Rfree (%) 21 / 25

Iron Binding Sites:

The binding sites of Iron atom in the 1.4 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixis at pH=5.6. (pdb code 1d3s). 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 1.4 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixis at pH=5.6., PDB code: 1d3s:

Iron binding site 1 out of 1 in 1d3s

Go back to Iron Binding Sites List in 1d3s
Iron binding site 1 out of 1 in the 1.4 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixis at pH=5.6.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.4 A Crystal Structure of Nitrophorin 4 From Rhodnius Prolixis at pH=5.6. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe185

b:9.0
occ:1.00
FE A:HEM185 0.0 9.0 1.0
NC A:HEM185 1.9 8.1 0.6
NB A:HEM185 1.9 8.1 0.5
NC A:HEM185 2.0 7.8 0.5
NB A:HEM185 2.0 7.8 0.6
NE2 A:HIS59 2.0 8.6 1.0
NA A:HEM185 2.0 5.3 0.5
ND A:HEM185 2.0 5.3 0.6
NA A:HEM185 2.0 10.2 0.6
ND A:HEM185 2.0 10.2 0.5
O A:HOH186 2.1 10.8 1.0
C1C A:HEM185 3.0 7.6 0.6
C4B A:HEM185 3.0 7.6 0.5
CD2 A:HIS59 3.0 10.0 1.0
C1C A:HEM185 3.0 8.7 0.5
C4B A:HEM185 3.0 8.7 0.6
C4C A:HEM185 3.0 9.5 0.6
C1B A:HEM185 3.0 9.5 0.5
CE1 A:HIS59 3.0 5.7 1.0
C1A A:HEM185 3.1 7.9 0.5
C4D A:HEM185 3.1 7.9 0.6
C1D A:HEM185 3.1 12.3 0.5
C4A A:HEM185 3.1 12.3 0.6
C4C A:HEM185 3.1 12.2 0.5
C1B A:HEM185 3.1 12.2 0.6
C1D A:HEM185 3.1 7.7 0.6
C4A A:HEM185 3.1 7.7 0.5
C1A A:HEM185 3.1 8.8 0.6
C4D A:HEM185 3.1 8.8 0.5
CHC A:HEM185 3.3 8.1 1.0
CHA A:HEM185 3.4 7.9 1.0
CHB A:HEM185 3.4 8.8 0.6
CHD A:HEM185 3.4 8.8 0.5
CHB A:HEM185 3.4 9.2 0.5
CHD A:HEM185 3.4 9.2 0.6
O A:HOH238 4.1 18.4 1.0
ND1 A:HIS59 4.1 6.6 1.0
CG A:HIS59 4.1 6.9 1.0
C3B A:HEM185 4.2 11.6 0.6
C2C A:HEM185 4.2 11.6 0.5
C3B A:HEM185 4.2 9.4 0.5
C2C A:HEM185 4.2 9.4 0.6
C2B A:HEM185 4.2 8.4 0.5
C3C A:HEM185 4.2 8.4 0.6
C2B A:HEM185 4.3 8.5 0.6
C3C A:HEM185 4.3 8.5 0.5
C2A A:HEM185 4.3 10.2 0.5
C3D A:HEM185 4.3 10.2 0.6
C3A A:HEM185 4.3 8.9 0.5
C2D A:HEM185 4.3 8.9 0.6
C3A A:HEM185 4.3 8.7 0.6
C2D A:HEM185 4.3 8.7 0.5
C2A A:HEM185 4.3 10.3 0.6
C3D A:HEM185 4.3 10.3 0.5
CD2 A:LEU133 5.0 27.5 1.0

Reference:

A.Weichsel, J.F.Andersen, S.A.Roberts, W.R.Montfort. Nitric Oxide Binding to Nitrophorin 4 Induces Complete Distal Pocket Burial. Nat.Struct.Biol. V. 7 551 2000.
ISSN: ISSN 1072-8368
PubMed: 10876239
DOI: 10.1038/76769
Page generated: Sun Dec 13 14:10:04 2020

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