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Structure of leucyl aminopeptidase from leishmania major in complex with actinonin

Analyse Structure of leucyl aminopeptidase from leishmania major in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NTH
Type: protein
Length: 537 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative aminopeptidase
EC: 3.4.11.-
UniProt: Q4QH17
Ligands: BCT, BB2, MN
Pockets: 4 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative aminopeptidase (EC 3.4.11.-)	protein	537	38% helix, 20% strand	Q4QH17

Ligands and binding sites

BCT · Bicarbonate ion · ligand · chains A
BB2 · Actinonin · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	173	0.56	0.81	29	empty
2	218	0.51	0.76	35	BB2
3	131	0.46	0.77	32	empty
4	51	0.29	0.75	16	empty

Compared structures

5NTH · Structure of Leucyl aminopeptidase from Leishmania major in complex with actinonin · 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 Q4QH17
Elsewhere: RCSB PDB 5NTH · PDBe 5NTH · UniProt Q4QH17

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