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The crystal structure of substrate-free CYP107X1 from Streptomyces avermitilis

Analyse The crystal structure of substrate-free CYP107X1 from Streptomyces avermitilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7WEX
Type: protein
Length: 382 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.99
Source: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893…
Molecule: Cytochrome P450 hydroxylase
UniProt: Q82A10
Ligands: HEM
Pockets: 2 · best druggability 0.85

Structure

x-ray diffraction · resolution 1.99 · 1 distinct chain · 52% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 hydroxylase	protein	382	52% helix, 10% strand	Q82A10

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
GOL · Glycerol · additive · 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	1124	0.85	0.86	88	HEM, GOL
2	103	0.39	0.76	16	empty

Compared structures

7WEX · The crystal structure of substrate-free CYP107X1 from streptomyces avermitilis · 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 Q82A10
Elsewhere: RCSB PDB 7WEX · PDBe 7WEX · UniProt Q82A10

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