MolNFT v1 · #118280 · protein

Structure of P450 staf from glycopeptide antibiotic A47934 biosynthesis; ethylene glycol cryo

5EX8 · Cytochrome P450: “Structure of P450 staf from glycopeptide antibiotic A47934 biosynthesis; ethylene glycol cryo”. X-ray diffraction, 1 ligand (HEM), 2 pockets (best druggability 0.78). MolNFT v1 #118280 on GenesisL1: 3D structure…

PDB: 5EX8
Type: protein
Length: 414 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450
UniProt: Q8KLL7
Ligands: HEM
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450	protein	414	54% helix, 10% strand	Q8KLL7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
EDO · 1,2-ethanediol · additive · 16 copies · chains A

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

Pockets

2 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	809	0.78	0.81	82	HEM, EDO
2	163	0.46	0.76	21	empty

Compared structures

5EX8 · Structure of P450 StaF from glycopeptide antibiotic A47934 biosynthesis; ethylene glycol… · 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 Q8KLL7
Elsewhere: RCSB PDB 5EX8 · PDBe 5EX8 · UniProt Q8KLL7

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