Research workbench

ASP271ALA escherichia COLI aminopeptidase P

Analyse ASP271ALA escherichia COLI aminopeptidase P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BWU
Type: protein
Length: 440 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminopeptidase P
EC: 3.4.11.9
UniProt: P15034
Ligands: NA, MG
Pockets: 5 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminopeptidase P (EC 3.4.11.9)	protein	440	40% helix, 18% strand	P15034

Ligands and binding sites

NA · Sodium ion · metal · chains A
MG · Magnesium ion · metal · chains A
FLC · Citrate anion · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	132	0.45	0.77	18	empty
2	73	0.45	0.82	20	NA
3	84	0.35	0.75	17	empty
4	59	0.31	0.76	11	empty
5	56	0.28	0.74	17	empty

Compared structures

2BWU · Asp271Ala Escherichia coli Aminopeptidase P · the same entry in another collection · chain A against A, TM-score 1.00
P15034 · AlphaFold monomer V2.0 prediction for xaa-pro aminopeptidase (P15034) · 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 P15034
Elsewhere: RCSB PDB 2BWU · PDBe 2BWU · UniProt P15034

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