Atomistry » Iron » PDB 1sdl-1stq » 1spg
Atomistry »
  Iron »
    PDB 1sdl-1stq »
      1spg »

Iron in PDB 1spg: Carbonmonoxy Hemoglobin From the Teleost Fish Leiostomus Xanthurus

Protein crystallography data

The structure of Carbonmonoxy Hemoglobin From the Teleost Fish Leiostomus Xanthurus, PDB code: 1spg was solved by S.E.Mylvaganam, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.95
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.600, 75.600, 69.700, 90.00, 141.90, 90.00
R / Rfree (%) 19.1 / 24.5

Iron Binding Sites:

The binding sites of Iron atom in the Carbonmonoxy Hemoglobin From the Teleost Fish Leiostomus Xanthurus (pdb code 1spg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Carbonmonoxy Hemoglobin From the Teleost Fish Leiostomus Xanthurus, PDB code: 1spg:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1spg

Go back to Iron Binding Sites List in 1spg
Iron binding site 1 out of 2 in the Carbonmonoxy Hemoglobin From the Teleost Fish Leiostomus Xanthurus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Carbonmonoxy Hemoglobin From the Teleost Fish Leiostomus Xanthurus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe144

b:8.1
occ:1.00
FE A:HEM144 0.0 8.1 1.0
C A:CMO145 1.8 11.5 1.0
NC A:HEM144 2.0 11.2 1.0
ND A:HEM144 2.0 16.4 1.0
NE2 A:HIS89 2.0 6.8 1.0
NA A:HEM144 2.0 15.6 1.0
NB A:HEM144 2.0 12.9 1.0
O A:CMO145 2.9 15.7 1.0
CE1 A:HIS89 2.9 8.4 1.0
C4C A:HEM144 3.0 13.1 1.0
C1D A:HEM144 3.0 15.4 1.0
C1C A:HEM144 3.0 10.3 1.0
C1A A:HEM144 3.0 14.7 1.0
C4D A:HEM144 3.0 15.2 1.0
C4B A:HEM144 3.0 12.2 1.0
CD2 A:HIS89 3.1 7.6 1.0
C4A A:HEM144 3.1 14.1 1.0
C1B A:HEM144 3.1 12.4 1.0
CHD A:HEM144 3.3 14.5 1.0
CHC A:HEM144 3.3 9.2 1.0
CHA A:HEM144 3.3 15.0 1.0
CHB A:HEM144 3.5 11.3 1.0
ND1 A:HIS89 4.1 8.6 1.0
CG A:HIS89 4.2 6.6 1.0
C2A A:HEM144 4.2 14.3 1.0
C3C A:HEM144 4.2 10.7 1.0
C2C A:HEM144 4.2 10.0 1.0
C2D A:HEM144 4.2 15.9 1.0
C3D A:HEM144 4.3 16.6 1.0
C3B A:HEM144 4.3 13.4 1.0
C3A A:HEM144 4.3 13.5 1.0
C2B A:HEM144 4.3 14.5 1.0
NE2 A:HIS60 4.7 13.0 1.0

Iron binding site 2 out of 2 in 1spg

Go back to Iron Binding Sites List in 1spg
Iron binding site 2 out of 2 in the Carbonmonoxy Hemoglobin From the Teleost Fish Leiostomus Xanthurus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Carbonmonoxy Hemoglobin From the Teleost Fish Leiostomus Xanthurus within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe148

b:11.4
occ:1.00
FE B:HEM148 0.0 11.4 1.0
C B:CMO149 1.8 14.1 1.0
ND B:HEM148 1.9 14.4 1.0
NA B:HEM148 2.0 15.6 1.0
NC B:HEM148 2.0 15.2 1.0
NB B:HEM148 2.0 14.2 1.0
NE2 B:HIS92 2.1 13.7 1.0
O B:CMO149 3.0 15.4 1.0
C4D B:HEM148 3.0 15.4 1.0
CD2 B:HIS92 3.0 11.4 1.0
C1D B:HEM148 3.0 13.1 1.0
C1A B:HEM148 3.0 15.9 1.0
C4C B:HEM148 3.1 14.3 1.0
C4A B:HEM148 3.1 15.4 1.0
CE1 B:HIS92 3.1 15.0 1.0
C1B B:HEM148 3.1 13.7 1.0
C1C B:HEM148 3.1 13.8 1.0
C4B B:HEM148 3.1 15.1 1.0
CHA B:HEM148 3.3 14.4 1.0
CHD B:HEM148 3.4 13.3 1.0
CHB B:HEM148 3.5 14.6 1.0
CHC B:HEM148 3.5 13.2 1.0
CG B:HIS92 4.1 13.6 1.0
ND1 B:HIS92 4.2 12.9 1.0
C2D B:HEM148 4.2 14.1 1.0
C3D B:HEM148 4.2 15.4 1.0
C2A B:HEM148 4.2 18.4 1.0
C3A B:HEM148 4.3 17.0 1.0
C3C B:HEM148 4.3 12.9 1.0
C2B B:HEM148 4.3 14.1 1.0
C2C B:HEM148 4.3 11.6 1.0
C3B B:HEM148 4.3 15.5 1.0
NE2 B:HIS63 4.5 17.3 1.0
CG2 B:VAL67 4.7 2.5 1.0

Reference:

S.E.Mylvaganam, C.Bonaventura, J.Bonaventura, E.D.Getzoff. Structural Basis For the Root Effect in Haemoglobin. Nat.Struct.Biol. V. 3 275 1996.
ISSN: ISSN 1072-8368
PubMed: 8605630
DOI: 10.1038/NSB0396-275
Page generated: Sat Aug 3 14:48:43 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy