Iron in PDB 8eko: Sperm Whale Myoglobin Mutant L29H F33W F43H (F33W Cubmb)

The structure of Sperm Whale Myoglobin Mutant L29H F33W F43H (F33W Cubmb), PDB code: 8eko was solved by A.P.Ledray, S.Dwaraknath, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.61 / 1.34
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.059, 48.07, 77.739, 90, 90, 90
R / Rfree (%)	13.9 / 16.4

The binding sites of Iron atom in the Sperm Whale Myoglobin Mutant L29H F33W F43H (F33W Cubmb) (pdb code 8eko). 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 L29H F33W F43H (F33W Cubmb), PDB code: 8eko:

Iron binding site 1 out of 1 in the Sperm Whale Myoglobin Mutant L29H F33W F43H (F33W Cubmb)


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 L29H F33W F43H (F33W Cubmb) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:6.8 occ:1.00 FE A:HEM201 0.0 6.8 1.0 ND A:HEM201 2.0 7.4 1.0 NC A:HEM201 2.0 6.5 1.0 NB A:HEM201 2.0 6.5 1.0 NA A:HEM201 2.0 7.0 1.0 O A:HOH349 2.1 9.3 1.0 NE2 A:HIS93 2.2 6.8 1.0 C1D A:HEM201 3.0 7.4 1.0 C4D A:HEM201 3.0 8.0 1.0 C4C A:HEM201 3.0 7.1 1.0 C4B A:HEM201 3.1 6.5 1.0 C1A A:HEM201 3.1 7.2 1.0 C4A A:HEM201 3.1 6.7 1.0 C1C A:HEM201 3.1 6.5 1.0 C1B A:HEM201 3.1 5.8 1.0 CE1 A:HIS93 3.1 7.9 1.0 CD2 A:HIS93 3.2 6.5 1.0 CHD A:HEM201 3.4 8.1 1.0 CHC A:HEM201 3.4 6.5 1.0 CHA A:HEM201 3.4 8.3 1.0 CHB A:HEM201 3.4 6.8 1.0 ND1 A:HIS93 4.2 7.9 1.0 C3D A:HEM201 4.3 10.5 1.0 C2D A:HEM201 4.3 9.5 1.0 C3C A:HEM201 4.3 7.9 1.0 C3B A:HEM201 4.3 6.0 1.0 C3A A:HEM201 4.3 7.7 1.0 C2A A:HEM201 4.3 8.2 1.0 C2B A:HEM201 4.3 6.1 1.0 C2C A:HEM201 4.3 7.7 1.0 CG A:HIS93 4.3 7.0 1.0 O A:HOH381 4.4 21.1 1.0 NE2 A:HIS64 4.5 10.9 1.0 CG2 A:VAL68 4.6 7.8 1.0 CE1 A:HIS64 4.8 11.2 1.0

A.P.Ledray, S.Dwaraknath, K.Chakarawet, M.R.Sponholtz, C.Merchen, C.Van Stappen, G.Rao, R.D.Britt, Y.Lu. Tryptophan Can Promote Oxygen Reduction to Water in A Biosynthetic Model of Heme Copper Oxidases. Biochemistry 2022.
ISSN: ISSN 0006-2960
PubMed: 36215733
DOI: 10.1021/ACS.BIOCHEM.2C00300