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Iron in PDB 2spo: A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate

Protein crystallography data

The structure of A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate, PDB code: 2spo was solved by M.L.Quillin, R.M.Arduini, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 1.70
Space group P 6
Cell size a, b, c (Å), α, β, γ (°) 91.200, 91.200, 45.870, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate (pdb code 2spo). 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 A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate, PDB code: 2spo:

Iron binding site 1 out of 1 in 2spo

Go back to Iron Binding Sites List in 2spo
Iron binding site 1 out of 1 in the A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe154

b:13.5
occ:1.00
FE A:HEM154 0.0 13.5 1.0
ND A:HEM154 1.9 12.7 1.0
NA A:HEM154 2.0 12.3 1.0
NC A:HEM154 2.0 12.6 1.0
NB A:HEM154 2.0 11.8 1.0
O A:HOH155 2.1 13.1 1.0
NE2 A:HIS93 2.3 12.7 1.0
C1D A:HEM154 3.0 13.5 1.0
C1C A:HEM154 3.0 13.1 1.0
C4D A:HEM154 3.0 12.5 1.0
C1B A:HEM154 3.0 12.0 1.0
C4A A:HEM154 3.0 12.4 1.0
C4B A:HEM154 3.0 12.7 1.0
C4C A:HEM154 3.0 13.2 1.0
C1A A:HEM154 3.1 12.8 1.0
CD2 A:HIS93 3.2 13.4 1.0
CE1 A:HIS93 3.2 13.3 1.0
CHD A:HEM154 3.4 12.6 1.0
CHC A:HEM154 3.4 13.0 1.0
CHB A:HEM154 3.4 11.2 1.0
CHA A:HEM154 3.4 12.5 1.0
C2C A:HEM154 4.3 13.1 1.0
C3D A:HEM154 4.3 13.8 1.0
C2D A:HEM154 4.3 13.8 1.0
C3C A:HEM154 4.3 14.1 1.0
C2A A:HEM154 4.3 13.2 1.0
NE2 A:HIS64 4.3 15.9 1.0
C3B A:HEM154 4.3 12.5 1.0
ND1 A:HIS93 4.3 12.7 1.0
C2B A:HEM154 4.3 12.0 1.0
C3A A:HEM154 4.3 12.5 1.0
CG A:HIS93 4.3 13.0 1.0
CG2 A:VAL68 4.8 12.3 1.0
CE1 A:HIS64 4.8 17.0 1.0

Reference:

T.E.Carver, R.E.Brantley Jr., E.W.Singleton, R.M.Arduini, M.L.Quillin, G.N.Phillips Jr., J.S.Olson. A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate. J.Biol.Chem. V. 267 14443 1992.
ISSN: ISSN 0021-9258
PubMed: 1629229
Page generated: Thu Jul 17 04:02:25 2025

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