MolNFT v1 · #144986 · protein

Prolyl oligopeptidase mutant S477C from pyrococcus furiosus

6CAN · Prolyl endopeptidase: “Prolyl oligopeptidase mutant S477C from pyrococcus furiosus”. X-ray diffraction, 1 ligand (CL), 11 pockets (best druggability 0.73). MolNFT v1 #144986 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6CAN
Type: protein
Length: 1,232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prolyl endopeptidase
UniProt: Q51714
Ligands: CL
Pockets: 11 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Prolyl endopeptidase	protein	616	24% helix, 38% strand	Q51714

Ligands and binding sites

CL · Chloride ion · ion · 6 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	846	0.73	0.77	63	empty
2	735	0.73	0.79	74	empty
3	611	0.70	0.79	58	empty
4	649	0.69	0.77	81	CL
5	711	0.68	0.76	76	CL

Interfaces

1 interface between chains.

A–B · 480 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6CAN · Prolyl oligopeptidase mutant S477C from Pyrococcus furiosus · the same entry in another collection · chain B against B, 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 Q51714
Elsewhere: RCSB PDB 6CAN · PDBe 6CAN · UniProt Q51714

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