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Iron in PDB 7l3y: Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy)

Protein crystallography data

The structure of Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy), PDB code: 7l3y was solved by I.Petrik, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.02 / 1.18
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.845, 46.982, 78.034, 90, 90, 90
R / Rfree (%) 15.7 / 19

Other elements in 7l3y:

The structure of Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy) also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy) (pdb code 7l3y). 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 Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy), PDB code: 7l3y:

Iron binding site 1 out of 1 in 7l3y

Go back to Iron Binding Sites List in 7l3y
Iron binding site 1 out of 1 in the Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy)


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 Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe201

b:8.4
occ:1.00
FE A:HEM201 0.0 8.4 1.0
O1 A:PER202 1.9 10.1 0.5
ND A:HEM201 2.0 8.1 1.0
NA A:HEM201 2.0 8.4 1.0
NB A:HEM201 2.1 8.1 1.0
NC A:HEM201 2.1 7.8 1.0
NE2 A:HIS93 2.1 9.2 1.0
O2 A:PER202 3.0 11.6 0.5
C4D A:HEM201 3.0 8.2 1.0
C1D A:HEM201 3.0 8.6 1.0
C4B A:HEM201 3.0 8.5 1.0
CE1 A:HIS93 3.0 9.5 1.0
C1C A:HEM201 3.1 7.8 1.0
C1A A:HEM201 3.1 8.5 1.0
C4A A:HEM201 3.1 8.7 1.0
C4C A:HEM201 3.1 8.7 1.0
C1B A:HEM201 3.1 8.5 1.0
CD2 A:HIS93 3.2 9.3 1.0
CHA A:HEM201 3.4 8.0 1.0
CHD A:HEM201 3.4 8.7 1.0
CHC A:HEM201 3.4 8.2 1.0
CHB A:HEM201 3.4 8.4 1.0
ND1 A:HIS93 4.2 10.0 1.0
O A:HOH445 4.2 14.8 0.5
C3D A:HEM201 4.3 9.3 1.0
C2D A:HEM201 4.3 9.5 1.0
C3C A:HEM201 4.3 9.3 1.0
CG A:HIS93 4.3 10.1 1.0
C3A A:HEM201 4.3 9.4 1.0
C2A A:HEM201 4.3 9.5 1.0
C2B A:HEM201 4.3 9.2 1.0
C2C A:HEM201 4.3 8.6 1.0
C3B A:HEM201 4.3 9.2 1.0
CG2 A:VAL68 4.5 10.5 1.0
CE1 A:HIS64 4.5 15.4 1.0
O A:HOH303 4.7 14.3 0.2
NE2 A:HIS64 4.7 15.0 1.0
CD2 A:HIS97 5.0 12.0 1.0

Reference:

I.D.Petrik, R.Davydov, M.Kahle, B.Sandoval, S.Dwaraknath, P.Adelroth, B.Hoffman, Y.Lu. An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity By Tuning the Hydrogen-Bonding Network. Biochemistry 2021.
ISSN: ISSN 0006-2960
PubMed: 33464878
DOI: 10.1021/ACS.BIOCHEM.0C00852
Page generated: Thu Aug 8 06:55:37 2024

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