MolNFT v1 · #2207 · protein

Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by X-ray crystallography

1BPN: “Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine…”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.50). MolNFT v1 #2207 on GenesisL1: 3D structure, binding sites…

PDB: 1BPN
Type: protein
Length: 481 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Leucine aminopeptidase
EC: 3.4.11.1
UniProt: P00727
Ligands: ZN
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Leucine aminopeptidase (EC 3.4.11.1)	protein	481	39% helix, 21% strand	P00727

Ligands and binding sites

ZN · Zinc ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.50	0.75	40	ZN
2	122	0.41	0.75	19	empty
3	62	0.35	0.78	19	empty

Compared structures

1BPN · Differentiation and identification of the two catalytic metal binding sites in bovine… · the same entry in another collection · chain A against A, TM-score 1.00
P00727 · AlphaFold monomer V2.0 prediction for cytosol aminopeptidase (P00727) · 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 P00727
Elsewhere: RCSB PDB 1BPN · PDBe 1BPN · UniProt P00727

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