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Crystal structure of legionella pneumophila aminopeptidase a

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

PDB: 5ZI5
Type: protein
Length: 1,700 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminopeptidase N
EC: 3.4.11.2
UniProt: Q5ZVE3
Ligands: ZN
Pockets: 20 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aminopeptidase N (EC 3.4.11.2)	protein	850	43% helix, 22% strand	Q5ZVE3

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1008	0.83	0.84	110	empty
2	495	0.76	0.84	74	empty
3	428	0.73	0.83	48	empty
4	307	0.69	0.83	36	empty
5	496	0.69	0.79	50	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

5ZI5 · Crystal structure of Legionella pneumophila aminopeptidase A · 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 Q5ZVE3
Elsewhere: RCSB PDB 5ZI5 · PDBe 5ZI5 · UniProt Q5ZVE3

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