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Crystal structure of dimeric TMPEP1050 aminopeptidase

Analyse Crystal structure of dimeric TMPEP1050 aminopeptidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NE6
Type: protein
Length: 617 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminopeptidase
EC: 3.4.11.1
UniProt: Q9X0E0
Pockets: 3 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminopeptidase (EC 3.4.11.1)	protein	306	29% helix, 30% strand	Q9X0E0
B	Aminopeptidase (EC 3.4.11.1)	protein	311	29% helix, 30% strand	Q9X0E0

Ligands and binding sites

CIT · Citric acid · additive · 2 copies · chains A

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

Pockets

3 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	177	0.58	0.82	31	empty
2	59	0.35	0.78	18	empty
3	83	0.34	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 649 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5NE6 · Crystal structure of dimeric TmPep1050 aminopeptidase · 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 Q9X0E0
Elsewhere: RCSB PDB 5NE6 · PDBe 5NE6 · UniProt Q9X0E0

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