Iron in PDB 7kyr: Crystal Structure of I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin)

The structure of Crystal Structure of I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin), PDB code: 7kyr 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)	34.83 / 1.71
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.016, 31.728, 71.283, 90, 102.35, 90
R / Rfree (%)	16.6 / 21

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

Sodium

(Na)

1 atom

The binding sites of Iron atom in the Crystal Structure of I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin) (pdb code 7kyr). 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 I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin), PDB code: 7kyr:

Iron binding site 1 out of 1 in the Crystal Structure of I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin)


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 I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:17.5 occ:1.00 FE A:HEM201 0.0 17.5 1.0 NE2 A:HIS93 2.1 20.2 1.0 NA A:HEM201 2.2 20.1 1.0 NB A:HEM201 2.2 19.2 1.0 NC A:HEM201 2.2 20.0 1.0 ND A:HEM201 2.2 20.3 1.0 O A:HOH331 2.2 24.2 1.0 CE1 A:HIS93 3.0 23.5 1.0 C1A A:HEM201 3.1 20.6 1.0 C4C A:HEM201 3.1 23.8 1.0 C4B A:HEM201 3.1 23.3 1.0 C1D A:HEM201 3.1 24.0 1.0 C4D A:HEM201 3.1 21.9 1.0 C1B A:HEM201 3.1 19.8 1.0 C4A A:HEM201 3.1 24.5 1.0 C1C A:HEM201 3.1 20.8 1.0 CD2 A:HIS93 3.2 23.5 1.0 CHA A:HEM201 3.5 22.5 1.0 CHD A:HEM201 3.5 25.5 1.0 CHC A:HEM201 3.5 20.9 1.0 CHB A:HEM201 3.5 20.5 1.0 O A:HOH342 4.1 39.4 1.0 ND1 A:HIS93 4.2 21.1 1.0 C2A A:HEM201 4.3 22.4 1.0 CG A:HIS93 4.3 21.8 1.0 C3C A:HEM201 4.3 25.3 1.0 C3A A:HEM201 4.3 24.1 1.0 C2B A:HEM201 4.3 21.0 1.0 C2C A:HEM201 4.3 23.9 1.0 C3D A:HEM201 4.3 23.9 1.0 C3B A:HEM201 4.3 22.1 1.0 C2D A:HEM201 4.3 23.4 1.0 NE2 A:HIS64 4.4 21.3 1.0 CG2 A:VAL68 4.6 19.4 1.0 CE1 A:HIS64 4.8 24.3 1.0 CE1 A:HIS43 4.9 32.9 1.0

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