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Iron in PDB 2auo: Residue F4 Plays A Key Role in Modulating the Oxygen Affinity and Cooperatrivity in Scapharca Dimeric Hemoglobin

Protein crystallography data

The structure of Residue F4 Plays A Key Role in Modulating the Oxygen Affinity and Cooperatrivity in Scapharca Dimeric Hemoglobin, PDB code: 2auo was solved by J.E.Knapp, M.A.Bonham, Q.H.Gibson, J.C.Nichols, W.E.Royer Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.11 / 1.53
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 93.280, 44.000, 83.610, 90.00, 121.98, 90.00
R / Rfree (%) 19.6 / 21.6

Iron Binding Sites:

The binding sites of Iron atom in the Residue F4 Plays A Key Role in Modulating the Oxygen Affinity and Cooperatrivity in Scapharca Dimeric Hemoglobin (pdb code 2auo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Residue F4 Plays A Key Role in Modulating the Oxygen Affinity and Cooperatrivity in Scapharca Dimeric Hemoglobin, PDB code: 2auo:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2auo

Go back to Iron Binding Sites List in 2auo
Iron binding site 1 out of 2 in the Residue F4 Plays A Key Role in Modulating the Oxygen Affinity and Cooperatrivity in Scapharca Dimeric Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Residue F4 Plays A Key Role in Modulating the Oxygen Affinity and Cooperatrivity in Scapharca Dimeric Hemoglobin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe153

b:12.7
occ:1.00
FE A:HEM153 0.0 12.7 1.0
C A:CMO154 1.9 13.0 1.0
ND A:HEM153 2.0 13.0 1.0
NC A:HEM153 2.0 12.2 1.0
NA A:HEM153 2.0 12.0 1.0
NB A:HEM153 2.0 12.4 1.0
NE2 A:HIS101 2.1 11.1 1.0
C4D A:HEM153 3.0 13.4 1.0
C1A A:HEM153 3.0 12.5 1.0
C1D A:HEM153 3.1 13.2 1.0
C4C A:HEM153 3.1 13.6 1.0
C4B A:HEM153 3.1 12.2 1.0
C1B A:HEM153 3.1 12.0 1.0
C1C A:HEM153 3.1 13.1 1.0
C4A A:HEM153 3.1 12.2 1.0
CE1 A:HIS101 3.1 10.5 1.0
O A:CMO154 3.1 15.3 1.0
CD2 A:HIS101 3.1 12.2 1.0
CHA A:HEM153 3.4 12.9 1.0
CHD A:HEM153 3.4 13.4 1.0
CHC A:HEM153 3.4 12.9 1.0
CHB A:HEM153 3.5 12.0 1.0
ND1 A:HIS101 4.2 12.2 1.0
CG A:HIS101 4.3 11.6 1.0
C3D A:HEM153 4.3 14.4 1.0
C2A A:HEM153 4.3 12.2 1.0
C2D A:HEM153 4.3 13.9 1.0
C3A A:HEM153 4.3 12.1 1.0
C2B A:HEM153 4.3 12.8 1.0
C2C A:HEM153 4.3 13.0 1.0
C3B A:HEM153 4.3 13.1 1.0
C3C A:HEM153 4.3 13.7 1.0
CE1 A:HIS69 4.7 14.7 1.0
CD1 A:LEU73 4.7 16.3 1.0
CE2 A:PHE111 4.9 14.8 1.0

Iron binding site 2 out of 2 in 2auo

Go back to Iron Binding Sites List in 2auo
Iron binding site 2 out of 2 in the Residue F4 Plays A Key Role in Modulating the Oxygen Affinity and Cooperatrivity in Scapharca Dimeric Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Residue F4 Plays A Key Role in Modulating the Oxygen Affinity and Cooperatrivity in Scapharca Dimeric Hemoglobin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe153

b:8.5
occ:1.00
FE B:HEM153 0.0 8.5 1.0
C B:CMO154 1.9 11.5 1.0
NB B:HEM153 2.0 10.2 1.0
ND B:HEM153 2.0 10.6 1.0
NC B:HEM153 2.0 11.2 1.0
NA B:HEM153 2.0 10.1 1.0
NE2 B:HIS101 2.1 10.8 1.0
C4B B:HEM153 3.0 10.9 1.0
C4D B:HEM153 3.0 11.9 1.0
C1A B:HEM153 3.0 11.3 1.0
C1C B:HEM153 3.0 11.9 1.0
C1B B:HEM153 3.0 10.9 1.0
O B:CMO154 3.1 12.8 1.0
C4C B:HEM153 3.1 12.0 1.0
C1D B:HEM153 3.1 11.4 1.0
C4A B:HEM153 3.1 11.1 1.0
CE1 B:HIS101 3.1 11.2 1.0
CD2 B:HIS101 3.1 11.4 1.0
CHC B:HEM153 3.4 11.1 1.0
CHA B:HEM153 3.4 11.7 1.0
CHD B:HEM153 3.4 12.7 1.0
CHB B:HEM153 3.4 11.5 1.0
ND1 B:HIS101 4.2 10.9 1.0
CG B:HIS101 4.3 11.2 1.0
C3B B:HEM153 4.3 11.3 1.0
C2B B:HEM153 4.3 10.9 1.0
C2C B:HEM153 4.3 12.1 1.0
C3C B:HEM153 4.3 12.6 1.0
C3D B:HEM153 4.3 12.4 1.0
C2A B:HEM153 4.3 11.6 1.0
C2D B:HEM153 4.3 12.2 1.0
C3A B:HEM153 4.3 11.0 1.0
CD1 B:LEU73 4.8 14.8 1.0
CE1 B:HIS69 4.8 11.9 1.0
CE2 B:PHE111 4.9 13.4 1.0

Reference:

J.E.Knapp, M.A.Bonham, Q.H.Gibson, J.C.Nichols, W.E.Royer Jr.. Residue F4 Plays A Key Role in Modulating Oxygen Affinity and Cooperativity in Scapharca Dimeric Hemoglobin Biochemistry V. 44 14419 2005.
ISSN: ISSN 0006-2960
PubMed: 16262242
DOI: 10.1021/BI051052+
Page generated: Sat Aug 3 19:24:35 2024

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