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Crystal structure analysis of the X-prolyl dipeptidyl aminopeptidase from lactococcus lactis

Analyse Crystal structure analysis of the X-prolyl dipeptidyl aminopeptidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LNS
Type: protein
Length: 763 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: X-prolyl dipeptidyl aminopeptidase
EC: 3.4.14.11
UniProt: P22346
Pockets: 7 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	X-prolyl dipeptidyl aminopeptidase (EC 3.4.14.11)	protein	763	26% helix, 26% strand	P22346

Pockets

7 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	212	0.51	0.76	32	empty
2	207	0.48	0.75	27	empty
3	165	0.48	0.77	25	empty
4	136	0.44	0.76	24	empty
5	83	0.37	0.76	21	empty

Compared structures

1LNS · Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus… · the same entry in another collection · chain A against A, TM-score 1.00
P22346 · AlphaFold monomer V2.0 prediction for xaa-pro dipeptidyl-peptidase (P22346) · 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 P22346
Elsewhere: RCSB PDB 1LNS · PDBe 1LNS · UniProt P22346

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