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High resolution crystal structures of five distal histidine mutants of sperm whale myoglobin

Analyse High resolution crystal structures of five distal histidine mutants of sperm… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MGH
Type: protein
Length: 154 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myoglobin
UniProt: P02185
Ligands: HEM, SO4
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myoglobin	protein	154	81% helix, 0% strand	P02185

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	208	0.72	0.87	26	HEM

Compared structures

2MGH · High resolution crystal structures of five distal histidine mutants of sperm whale… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P02185
Elsewhere: RCSB PDB 2MGH · PDBe 2MGH · UniProt P02185

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