MolNFT v1 · #173070 · protein

Structure of CYP153A from polaromonas sp.

7ANT · Cytochrome P450: “Structure of CYP153A from polaromonas sp.”. X-ray diffraction, 1 ligand (HEC), 6 pockets (best druggability 0.86). MolNFT v1 #173070 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7ANT
Type: protein
Length: 796 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450
UniProt: Q11ZY2
Ligands: HEC
Pockets: 6 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450	protein	396	52% helix, 10% strand	Q11ZY2
B	Cytochrome P450	protein	400	50% helix, 10% strand	Q11ZY2

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 11 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	371	0.86	0.95	53	HEC
2	726	0.83	0.86	70	HEC, EDO
3	784	0.78	0.82	73	EDO
4	118	0.56	0.84	22	empty
5	142	0.50	0.79	30	EDO

Interfaces

1 interface between chains.

A–B · 1092 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

7ANT · Structure of CYP153A from Polaromonas sp. · 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 Q11ZY2
Elsewhere: RCSB PDB 7ANT · PDBe 7ANT · UniProt Q11ZY2

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