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Structure of CYP153A from marinobacter aquaeolei

Analyse Structure of CYP153A from marinobacter aquaeolei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FYF
Type: protein
Length: 831 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450
UniProt: A1TY82
Ligands: HEM
Pockets: 8 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450	protein	420	51% helix, 11% strand	A1TY82
B	Cytochrome P450	protein	411	52% helix, 11% strand	A1TY82

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	546	0.86	0.91	71	HEM
2	586	0.83	0.88	71	HEM
3	667	0.80	0.85	71	empty
4	315	0.72	0.85	50	empty
5	68	0.39	0.80	15	empty

Interfaces

1 interface between chains.

A–B · 540 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5FYF · Structure of CYP153A from Marinobacter aquaeolei · 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 A1TY82
Elsewhere: RCSB PDB 5FYF · PDBe 5FYF · UniProt A1TY82

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