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Crystal structures of the no-and co-bound heme oxygenase from neisseria meningitidis: implications for oxygen activation

Analyse Crystal structures of the no-and co-bound heme oxygenase from neisseria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1P3T
Type: protein
Length: 199 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heme oxygenase 1
EC: 1.14.99.3
UniProt: Q9RGD9
Ligands: HEM
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heme oxygenase 1 (EC 1.14.99.3)	protein	199	65% helix, 2% strand	Q9RGD9

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	265	0.69	0.84	32	HEM
2	94	0.44	0.80	18	empty

Compared structures

1P3T · Crystal Structures of the NO-and CO-Bound Heme Oxygenase From Neisseria Meningitidis… · 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 Q9RGD9
Elsewhere: RCSB PDB 1P3T · PDBe 1P3T · UniProt Q9RGD9

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