MolNFT v1 · #149618 · protein

The structure of a carbohydrate active P450

6G5Q · Cytochrome P450: “The structure of a carbohydrate active P450”. X-ray diffraction, 2 ligands (EMZ, HEM), 2 pockets (best druggability 0.84). MolNFT v1 #149618 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6G5Q
Type: protein
Length: 755 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450
EC: 1.14.15.-
UniProt: G0L713
Ligands: EMZ, HEM
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 (EC 1.14.15.-)	protein	374	49% helix, 17% strand	G0L713
B	Cytochrome P450 (EC 1.14.15.-)	protein	381	48% helix, 17% strand	G0L713

Ligands and binding sites

EMZ · 6-O-methyl-beta-D-galactopyranose · ligand · 2 copies · chains A, B
HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · chains B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	830	0.84	0.87	73	EMZ, HEM
2	896	0.81	0.83	78	EMZ, HEM

Interfaces

1 interface between chains.

A–B · 338 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6G5Q · The structure of a carbohydrate active P450 · 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 G0L713
Elsewhere: RCSB PDB 6G5Q · PDBe 6G5Q · UniProt G0L713

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