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Iron in PDB 1h1x: Sperm Whale Myoglobin Mutant T67R S92D

Protein crystallography data

The structure of Sperm Whale Myoglobin Mutant T67R S92D, PDB code: 1h1x was solved by S.Zuccotti, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.0 / 1.4
Space group P 6
Cell size a, b, c (Å), α, β, γ (°) 90.524, 90.524, 45.129, 90.00, 90.00, 120.00
R / Rfree (%) 11.9 / 15.3

Iron Binding Sites:

The binding sites of Iron atom in the Sperm Whale Myoglobin Mutant T67R S92D (pdb code 1h1x). 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 Sperm Whale Myoglobin Mutant T67R S92D, PDB code: 1h1x:

Iron binding site 1 out of 1 in 1h1x

Go back to Iron Binding Sites List in 1h1x
Iron binding site 1 out of 1 in the Sperm Whale Myoglobin Mutant T67R S92D


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sperm Whale Myoglobin Mutant T67R S92D within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1154

b:8.0
occ:1.00
FE A:HEM1154 0.0 8.0 1.0
C A:CYN1155 2.0 12.7 1.0
NB A:HEM1154 2.0 7.8 1.0
NA A:HEM1154 2.0 8.5 1.0
NC A:HEM1154 2.0 7.9 1.0
ND A:HEM1154 2.0 8.5 1.0
NE2 A:HIS93 2.1 8.7 1.0
C1A A:HEM1154 3.0 9.2 1.0
CE1 A:HIS93 3.0 9.2 1.0
C4B A:HEM1154 3.0 7.2 1.0
C1B A:HEM1154 3.0 8.1 1.0
C4A A:HEM1154 3.1 8.2 1.0
C1C A:HEM1154 3.1 7.4 1.0
C4C A:HEM1154 3.1 7.7 1.0
C4D A:HEM1154 3.1 8.1 1.0
C1D A:HEM1154 3.1 8.3 1.0
CD2 A:HIS93 3.1 9.2 1.0
N A:CYN1155 3.2 9.9 1.0
CHC A:HEM1154 3.4 7.8 1.0
CHB A:HEM1154 3.4 8.2 1.0
CHD A:HEM1154 3.4 8.9 1.0
CHA A:HEM1154 3.4 9.2 1.0
ND1 A:HIS93 4.2 9.6 1.0
CG A:HIS93 4.2 7.3 1.0
C2A A:HEM1154 4.3 8.8 1.0
C3A A:HEM1154 4.3 8.2 1.0
C3B A:HEM1154 4.3 8.5 1.0
C3C A:HEM1154 4.3 9.2 1.0
C2C A:HEM1154 4.3 9.6 1.0
C2B A:HEM1154 4.3 8.3 1.0
C3D A:HEM1154 4.3 9.5 1.0
C2D A:HEM1154 4.3 10.0 1.0
CG2 A:VAL68 4.7 9.9 1.0
CE1 A:HIS64 4.8 12.1 1.0
NE2 A:HIS64 4.9 11.6 1.0

Reference:

R.Roncone, E.Monzani, M.Murtas, G.Battaini, A.Pennati, A.M.Sanangelantoni, S.Zuccotti, M.Bolognesi, L.Casella. Engineering Peroxidase Activity in Myoglobin: the Haem Cavity Structure and Peroxide Activation in the T67R/S92D Mutant and Its Derivative Reconstituted with Protohaemin-L-Histidine. Biochem.J. V. 377 717 2004.
ISSN: ISSN 0264-6021
PubMed: 14563209
DOI: 10.1042/BJ20030863
Page generated: Sun Dec 13 14:16:31 2020

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