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Iron in PDB 7spf: Crystal Structure of Sperm Whale Myoglobin Variant SMB5(Pcaaf)

Protein crystallography data

The structure of Crystal Structure of Sperm Whale Myoglobin Variant SMB5(Pcaaf), PDB code: 7spf was solved by J.P.Bacik, R.Fasan, N.Ando, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.66 / 1.17
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.408, 55.985, 65.855, 90, 90, 90
R / Rfree (%) 14.7 / 17.2

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Sperm Whale Myoglobin Variant SMB5(Pcaaf) (pdb code 7spf). 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 Crystal Structure of Sperm Whale Myoglobin Variant SMB5(Pcaaf), PDB code: 7spf:

Iron binding site 1 out of 1 in 7spf

Go back to Iron Binding Sites List in 7spf
Iron binding site 1 out of 1 in the Crystal Structure of Sperm Whale Myoglobin Variant SMB5(Pcaaf)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Sperm Whale Myoglobin Variant SMB5(Pcaaf) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe202

b:9.7
occ:1.00
FE A:HEM202 0.0 9.7 1.0
NC A:HEM202 2.0 9.9 1.0
NB A:HEM202 2.0 9.8 1.0
ND A:HEM202 2.0 9.9 1.0
NA A:HEM202 2.0 10.2 1.0
NE2 A:HIS93 2.1 9.9 1.0
O2 A:OXY203 2.1 14.4 1.0
CE1 A:HIS93 3.0 10.9 1.0
C4D A:HEM202 3.0 10.4 1.0
C4B A:HEM202 3.0 9.7 1.0
C4A A:HEM202 3.1 10.4 1.0
C1D A:HEM202 3.1 9.9 1.0
C1B A:HEM202 3.1 9.7 1.0
C1C A:HEM202 3.1 10.0 1.0
C4C A:HEM202 3.1 9.8 1.0
O1 A:OXY203 3.1 19.1 1.0
C1A A:HEM202 3.1 10.5 1.0
CD2 A:HIS93 3.1 10.7 1.0
CHD A:HEM202 3.4 10.0 1.0
CHB A:HEM202 3.4 10.0 1.0
CHC A:HEM202 3.4 10.0 1.0
CHA A:HEM202 3.4 10.5 1.0
ND1 A:HIS93 4.2 11.5 1.0
CG A:HIS93 4.2 10.9 1.0
C3A A:HEM202 4.3 11.1 1.0
C3D A:HEM202 4.3 10.5 1.0
C2A A:HEM202 4.3 11.1 1.0
C3B A:HEM202 4.3 10.4 1.0
C2B A:HEM202 4.3 10.1 1.0
C2D A:HEM202 4.3 10.2 1.0
C3C A:HEM202 4.3 9.8 1.0
C2C A:HEM202 4.3 10.2 1.0
O A:HOH358 4.3 15.2 1.0
CD2 A:HIS97 5.0 12.2 1.0

Reference:

J.A.Iannuzzelli, J.P.Bacik, E.J.Moore, Z.Shen, E.M.Irving, D.A.Vargas, S.D.Khare, N.Ando, R.Fasan. Tuning Enzyme Thermostability Via Computationally Guided Covalent Stapling and Structural Basis of Enhanced Stabilization. Biochemistry V. 61 1041 2022.
ISSN: ISSN 0006-2960
PubMed: 35612958
DOI: 10.1021/ACS.BIOCHEM.2C00033
Page generated: Fri Aug 9 00:56:00 2024

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