Atomistry » Iron » PDB 1rak-1rsv » 1rps
Atomistry »
  Iron »
    PDB 1rak-1rsv »
      1rps »

Iron in PDB 1rps: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions

Protein crystallography data

The structure of Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions, PDB code: 1rps was solved by N.-L.Chan, J.S.Kavanaugh, P.H.Rogers, A.Arnone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.11
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 97.000, 99.300, 66.100, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 23.2

Iron Binding Sites:

The binding sites of Iron atom in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions (pdb code 1rps). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions, PDB code: 1rps:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1rps

Go back to Iron Binding Sites List in 1rps
Iron binding site 1 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe142

b:19.6
occ:1.00
FE A:HEM142 0.0 19.6 1.0
N A:NO150 1.7 20.6 1.0
ND A:HEM142 2.0 20.2 1.0
NC A:HEM142 2.0 20.5 1.0
NA A:HEM142 2.0 20.2 1.0
NB A:HEM142 2.1 18.0 1.0
O A:NO150 2.7 22.4 1.0
C1D A:HEM142 3.0 19.5 1.0
C4C A:HEM142 3.0 19.4 1.0
C1A A:HEM142 3.0 19.5 1.0
C4D A:HEM142 3.0 19.6 1.0
C1C A:HEM142 3.1 17.6 1.0
C4B A:HEM142 3.1 18.0 1.0
C4A A:HEM142 3.1 20.2 1.0
C1B A:HEM142 3.1 18.0 1.0
CHD A:HEM142 3.3 19.7 1.0
CHA A:HEM142 3.4 19.9 1.0
CHC A:HEM142 3.4 18.4 1.0
CHB A:HEM142 3.5 16.2 1.0
CE1 A:HIS87 3.9 23.5 1.0
NE2 A:HIS58 4.1 22.3 1.0
NE2 A:HIS87 4.1 21.9 1.0
C3C A:HEM142 4.2 19.0 1.0
C2D A:HEM142 4.2 20.8 1.0
C2A A:HEM142 4.2 21.3 1.0
C2C A:HEM142 4.2 18.7 1.0
C3D A:HEM142 4.3 22.9 1.0
C3A A:HEM142 4.3 21.6 1.0
C3B A:HEM142 4.3 17.4 1.0
C2B A:HEM142 4.3 18.2 1.0
CD1 A:LEU91 4.8 25.3 1.0
CG2 A:VAL62 4.8 23.0 1.0
CE1 A:HIS58 4.9 22.3 1.0

Iron binding site 2 out of 4 in 1rps

Go back to Iron Binding Sites List in 1rps
Iron binding site 2 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe147

b:17.2
occ:1.00
FE B:HEM147 0.0 17.2 1.0
N B:NO150 1.7 16.6 1.0
NC B:HEM147 2.0 16.5 1.0
ND B:HEM147 2.0 14.4 1.0
NB B:HEM147 2.0 14.2 1.0
NA B:HEM147 2.1 15.5 1.0
NE2 B:HIS92 2.2 13.5 1.0
O B:NO150 2.7 19.3 1.0
C4C B:HEM147 2.9 15.9 1.0
C1C B:HEM147 3.0 14.4 1.0
C1D B:HEM147 3.0 15.4 1.0
C4B B:HEM147 3.0 14.1 1.0
C4D B:HEM147 3.0 13.9 1.0
C1A B:HEM147 3.0 16.1 1.0
C1B B:HEM147 3.1 16.0 1.0
C4A B:HEM147 3.1 13.9 1.0
CE1 B:HIS92 3.1 13.6 1.0
CD2 B:HIS92 3.3 14.7 1.0
CHC B:HEM147 3.3 11.8 1.0
CHD B:HEM147 3.3 14.0 1.0
CHA B:HEM147 3.4 15.1 1.0
CHB B:HEM147 3.5 14.5 1.0
C3C B:HEM147 4.1 16.6 1.0
C2C B:HEM147 4.1 16.5 1.0
C2D B:HEM147 4.2 15.1 1.0
C3B B:HEM147 4.3 13.7 1.0
C3D B:HEM147 4.3 17.2 1.0
NE2 B:HIS63 4.3 18.0 1.0
C2A B:HEM147 4.3 13.1 1.0
ND1 B:HIS92 4.3 13.4 1.0
C3A B:HEM147 4.3 13.4 1.0
C2B B:HEM147 4.3 15.2 1.0
CG B:HIS92 4.4 15.1 1.0
CG2 B:VAL67 4.5 22.1 1.0

Iron binding site 3 out of 4 in 1rps

Go back to Iron Binding Sites List in 1rps
Iron binding site 3 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe142

b:19.9
occ:1.00
FE C:HEM142 0.0 19.9 1.0
N C:NO150 1.7 21.9 1.0
ND C:HEM142 2.0 21.4 1.0
NB C:HEM142 2.0 21.6 1.0
NC C:HEM142 2.0 20.9 1.0
NA C:HEM142 2.1 22.8 1.0
O C:NO150 2.6 22.4 1.0
C1D C:HEM142 3.0 21.0 1.0
C4D C:HEM142 3.0 20.7 1.0
C1B C:HEM142 3.0 22.7 1.0
C4C C:HEM142 3.0 17.9 1.0
C4B C:HEM142 3.0 22.5 1.0
C1C C:HEM142 3.0 20.4 1.0
C1A C:HEM142 3.1 21.3 1.0
C4A C:HEM142 3.1 20.3 1.0
CHD C:HEM142 3.4 18.2 1.0
CHA C:HEM142 3.4 21.7 1.0
CHB C:HEM142 3.4 22.4 1.0
CHC C:HEM142 3.4 20.9 1.0
CE1 C:HIS87 3.8 28.9 1.0
NE2 C:HIS87 4.0 29.5 1.0
C3C C:HEM142 4.2 17.3 1.0
C2B C:HEM142 4.2 24.7 1.0
NE2 C:HIS58 4.2 24.5 1.0
C2D C:HEM142 4.2 21.8 1.0
C3D C:HEM142 4.2 20.7 1.0
C2C C:HEM142 4.2 21.4 1.0
C3B C:HEM142 4.2 22.9 1.0
C2A C:HEM142 4.3 25.8 1.0
C3A C:HEM142 4.3 24.4 1.0
CG2 C:VAL62 4.8 24.8 1.0
CE1 C:HIS58 4.8 26.8 1.0
CD1 C:LEU91 5.0 22.9 1.0

Iron binding site 4 out of 4 in 1rps

Go back to Iron Binding Sites List in 1rps
Iron binding site 4 out of 4 in the Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin Exposed to No Under Anerobic Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe147

b:24.8
occ:1.00
FE D:HEM147 0.0 24.8 1.0
N D:NO150 1.7 25.0 1.0
ND D:HEM147 2.0 24.9 1.0
NC D:HEM147 2.0 23.1 1.0
NB D:HEM147 2.0 24.5 1.0
NA D:HEM147 2.0 25.3 1.0
NE2 D:HIS92 2.2 23.3 1.0
O D:NO150 2.5 27.1 1.0
C1D D:HEM147 3.0 27.0 1.0
C4C D:HEM147 3.0 24.6 1.0
C4D D:HEM147 3.0 26.5 1.0
C1B D:HEM147 3.0 26.1 1.0
C1C D:HEM147 3.0 23.9 1.0
C4B D:HEM147 3.0 24.0 1.0
C1A D:HEM147 3.1 27.1 1.0
C4A D:HEM147 3.1 25.5 1.0
CE1 D:HIS92 3.2 24.9 1.0
CD2 D:HIS92 3.2 24.5 1.0
CHD D:HEM147 3.3 28.0 1.0
CHC D:HEM147 3.4 22.3 1.0
CHA D:HEM147 3.4 25.8 1.0
CHB D:HEM147 3.4 26.1 1.0
C2D D:HEM147 4.2 26.3 1.0
C2B D:HEM147 4.2 24.4 1.0
C3C D:HEM147 4.2 24.5 1.0
C3B D:HEM147 4.2 24.2 1.0
C2C D:HEM147 4.2 24.1 1.0
C3D D:HEM147 4.2 28.0 1.0
C2A D:HEM147 4.3 29.0 1.0
C3A D:HEM147 4.3 27.6 1.0
ND1 D:HIS92 4.3 25.4 1.0
CG D:HIS92 4.4 25.4 1.0
NE2 D:HIS63 4.5 27.1 1.0
CG2 D:VAL67 4.6 27.3 1.0

Reference:

N.-L.Chan, J.S.Kavanaugh, P.H.Rogers, A.Arnone. Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Biochemistry V. 43 118 2004.
ISSN: ISSN 0006-2960
PubMed: 14705937
DOI: 10.1021/BI0497603
Page generated: Sat Aug 3 14:19:09 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