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Iron in PDB 3sdn: Structure of G65I Sperm Whale Myoglobin Mutant

Protein crystallography data

The structure of Structure of G65I Sperm Whale Myoglobin Mutant, PDB code: 3sdn was solved by L.Lebioda, X.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.82 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.036, 48.011, 77.557, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 23.8

Iron Binding Sites:

The binding sites of Iron atom in the Structure of G65I Sperm Whale Myoglobin Mutant (pdb code 3sdn). 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 Structure of G65I Sperm Whale Myoglobin Mutant, PDB code: 3sdn:

Iron binding site 1 out of 1 in 3sdn

Go back to Iron Binding Sites List in 3sdn
Iron binding site 1 out of 1 in the Structure of G65I Sperm Whale Myoglobin Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of G65I Sperm Whale Myoglobin Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe160

b:14.6
occ:1.00
FE A:HEM160 0.0 14.6 1.0
NC A:HEM160 1.9 11.1 1.0
NB A:HEM160 2.0 13.1 1.0
NA A:HEM160 2.0 13.3 1.0
ND A:HEM160 2.0 13.9 1.0
NE2 A:HIS93 2.2 14.6 1.0
O A:ACT165 2.4 21.6 1.0
C1C A:HEM160 3.0 13.8 1.0
C1B A:HEM160 3.0 12.3 1.0
C1D A:HEM160 3.0 14.8 1.0
C4C A:HEM160 3.0 12.4 1.0
C1A A:HEM160 3.0 16.0 1.0
C4A A:HEM160 3.1 12.4 1.0
C4B A:HEM160 3.1 13.4 1.0
CE1 A:HIS93 3.1 16.6 1.0
C4D A:HEM160 3.1 14.6 1.0
CD2 A:HIS93 3.2 15.1 1.0
CHB A:HEM160 3.4 13.4 1.0
CHC A:HEM160 3.4 14.1 1.0
C A:ACT165 3.4 21.9 1.0
CHD A:HEM160 3.4 13.8 1.0
CHA A:HEM160 3.4 15.9 1.0
CH3 A:ACT165 4.0 22.1 1.0
C2C A:HEM160 4.2 14.2 1.0
ND1 A:HIS93 4.2 14.1 1.0
C3C A:HEM160 4.3 14.7 1.0
C3B A:HEM160 4.3 14.1 1.0
C3A A:HEM160 4.3 15.9 1.0
C2B A:HEM160 4.3 12.7 1.0
C2D A:HEM160 4.3 14.6 1.0
C2A A:HEM160 4.3 14.8 1.0
CG A:HIS93 4.3 12.8 1.0
C3D A:HEM160 4.3 16.4 1.0
OXT A:ACT165 4.5 21.0 1.0
CG2 A:VAL68 4.7 14.2 1.0
O A:HOH424 5.0 42.8 1.0
CE1 A:HIS64 5.0 19.4 1.0

Reference:

J.Du, X.Huang, S.Sun, C.Wang, L.Lebioda, J.H.Dawson. Amphitrite Ornata Dehaloperoxidase (Dhp): Investigations of Structural Factors That Influence the Mechanism of Halophenol Dehalogenation Using "Peroxidase-Like" Myoglobin Mutants and "Myoglobin-Like" Dhp Mutants. Biochemistry V. 50 8172 2011.
ISSN: ISSN 0006-2960
PubMed: 21800850
DOI: 10.1021/BI2009129
Page generated: Sun Aug 4 19:54:58 2024

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