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Prolyl oligopeptidase from porcine brain

Analyse Prolyl oligopeptidase from porcine brain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H2W
Type: protein
Length: 710 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prolyl endopeptidase
EC: 3.4.21.26
UniProt: P23687
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prolyl endopeptidase (EC 3.4.21.26)	protein	710	23% helix, 33% strand	P23687

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

7 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	1033	0.76	0.78	103	empty
2	482	0.67	0.78	42	empty
3	92	0.50	0.82	23	empty
4	98	0.40	0.77	18	empty
5	59	0.30	0.75	19	empty

Compared structures

1H2W · Prolyl oligopeptidase from porcine brain · the same entry in another collection · chain A against A, TM-score 1.00
P23687 · AlphaFold monomer V2.0 prediction for prolyl endopeptidase (P23687) · a predicted model of the same protein · 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 P23687
Elsewhere: RCSB PDB 1H2W · PDBe 1H2W · UniProt P23687

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