MolNFT v1 · #1331 · protein

Human procarboxypeptidase A2

1AYE: “Human procarboxypeptidase A2”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.78). MolNFT v1 #1331 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1AYE
Type: protein
Length: 401 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Procarboxypeptidase A2
EC: 3.4.17.15
UniProt: P48052
Ligands: ZN
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Procarboxypeptidase A2 (EC 3.4.17.15)	protein	401	41% helix, 18% strand	P48052

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

2 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	773	0.78	0.82	81	empty
2	68	0.40	0.79	19	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1AYE · Human procarboxypeptidase A2 · the same entry in another collection · chain A against A, TM-score 1.00
P48052 · AlphaFold monomer V2.0 prediction for carboxypeptidase A2 (P48052) · 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 P48052
Elsewhere: RCSB PDB 1AYE · PDBe 1AYE · UniProt P48052

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