MolNFT v1 · #188468 · protein

P450 (oxya) from kistamicin biosynthesis, mixed heme conformation, attenuated beam

7TTA · Putative cytochrome P450 hydroxylase: “P450 (oxya) from kistamicin biosynthesis, mixed heme conformation, attenuated beam”. X-ray diffraction, 1 ligand (HEM), 1 pocket (best druggability 0.79). MolNFT v1 #188468 on GenesisL1: 3D…

PDB: 7TTA
Type: protein
Length: 354 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative cytochrome P450 hydroxylase
UniProt: A0A2P9IBF7
Ligands: HEM
Pockets: 1 · best druggability 0.79

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative cytochrome P450 hydroxylase	protein	354	54% helix, 11% strand	A0A2P9IBF7

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	495	0.79	0.86	63	HEM

Compared structures

7TTA · P450 (OxyA) from kistamicin biosynthesis, mixed heme conformation, attenuated beam · 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 7TTA · PDBe 7TTA · UniProt A0A2P9IBF7

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