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Crystal structures of the G139A, G139A-no and G143H mutants of human heme oxygenase-1

Analyse Crystal structures of the G139A, G139A-no and G143H mutants of human heme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XK0
Type: protein
Length: 428 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heme oxygenase 1
EC: 1.14.99.3
UniProt: P09601
Ligands: HEM, NO
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Heme oxygenase 1 (EC 1.14.99.3)	protein	214	76% helix, 0% strand	P09601

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
NO · Nitric oxide · ion · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	345	0.72	0.84	37	HEM
2	379	0.72	0.83	40	HEM, NO

Compared structures

1XK0 · Crystal Structures of the G139A, G139A-NO and G143H Mutants of Human Heme Oxygenase-1 · the same entry in another collection · chain A against A, TM-score 1.00
P09601 · AlphaFold monomer V2.0 prediction for heme oxygenase 1 (P09601) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P09601
Elsewhere: RCSB PDB 1XK0 · PDBe 1XK0 · UniProt P09601

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