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P450 (oxya) from kistamicin biosynthesis, imidazole complex

Analyse P450 (oxya) from kistamicin biosynthesis, imidazole complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TTQ
Type: protein
Length: 357 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 hydroxylase
EC: 1.-.-.-
UniProt: A0A2P9IBF7
Ligands: HEM
Pockets: 3 · best druggability 0.80

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 hydroxylase (EC 1.-.-.-)	protein	357	54% helix, 11% strand	A0A2P9IBF7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
IMD · Imidazole · additive · chains A
GOL · Glycerol · additive · chains A

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

Pockets

3 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	534	0.80	0.86	65	IMD, HEM
2	50	0.40	0.82	13	empty
3	50	0.28	0.75	14	empty

Compared structures

7TTQ · P450 (OxyA) from kistamicin biosynthesis, imidazole complex · 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 A0A2P9IBF7
Elsewhere: RCSB PDB 7TTQ · PDBe 7TTQ · UniProt A0A2P9IBF7

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