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Crystal structure of prolyl aminopeptidase, complex with pro-tboda

Analyse Crystal structure of prolyl aminopeptidase, complex with pro-tboda in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WM1
Type: protein
Length: 313 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proline iminopeptidase
EC: 3.4.11.5
UniProt: O32449
Ligands: PTB
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proline iminopeptidase (EC 3.4.11.5)	protein	313	45% helix, 16% strand	O32449

Ligands and binding sites

PTB · (5-tert-butyl-1,3,4-oxadiazol-2-yl)[(2r)-pyrrolidin-2-yl]methanone · ligand · 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	343	0.68	0.82	37	PTB

Compared structures

1WM1 · Crystal Structure of Prolyl Aminopeptidase, Complex with Pro-TBODA · the same entry in another collection · chain A against A, TM-score 1.00
O32449 · AlphaFold monomer V2.0 prediction for proline iminopeptidase (O32449) · 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 O32449
Elsewhere: RCSB PDB 1WM1 · PDBe 1WM1 · UniProt O32449

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