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Crystal structure of CYP154C2 from streptomyces avermitilis

Analyse Crystal structure of CYP154C2 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: 6L69
Type: protein
Length: 796 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 hydroxylase
UniProt: Q82GL5
Ligands: HEM
Pockets: 9 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cytochrome P450 hydroxylase	protein	398	54% helix, 11% strand	Q82GL5

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	486	0.85	0.92	59	HEM
2	513	0.84	0.91	58	HEM
3	414	0.65	0.79	35	empty
4	303	0.64	0.80	35	empty
5	226	0.60	0.81	28	empty

Interfaces

1 interface between chains.

A–B · 284 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6L69 · Crystal structure of CYP154C2 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 Q82GL5
Elsewhere: RCSB PDB 6L69 · PDBe 6L69 · UniProt Q82GL5

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