MolNFT v1 · #10353 · protein

Incorporation of a hemin with the shortest acid side-chains into myoglobin

1IOP: “Incorporation of a hemin with the shortest acid side-chains into myoglobin”. X-ray diffraction, 3 ligands (HE6, CYN, SO4), 1 pocket (best druggability 0.74). MolNFT v1 #10353 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1IOP
Type: protein
Length: 153 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myoglobin
UniProt: P02185
Ligands: HE6, CYN, SO4
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myoglobin	protein	153	75% helix, 0% strand	P02185

Ligands and binding sites

HE6 · 6,7-dicarboxyl-1,2,3,4,5,8-hexamethylhemin · ligand · chains A
CYN · Cyanide ion · ion · 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	245	0.74	0.88	33	CYN, HE6

Compared structures

1IOP · Incorporation of a hemin with the shortest acid side-chains into myoglobin · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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 1IOP · PDBe 1IOP · UniProt P02185

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