MolNFT v1 · #115625 · protein

Refined crystal structure of carboxypeptidase a at 1.54 ångströms resolution.

5CPA: “Refined crystal structure of carboxypeptidase a at 1.54 ångströms resolution.”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.58). MolNFT v1 #115625 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5CPA
Type: protein
Length: 307 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxypeptidase a
EC: 3.4.17.1
UniProt: P00730
Ligands: ZN
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxypeptidase a (EC 3.4.17.1)	protein	307	38% helix, 17% strand	P00730

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	181	0.58	0.82	30	empty
2	51	0.35	0.79	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5CPA · Refined crystal structure of carboxypeptidase a at 1.54 ångströms resolution. · the same entry in another collection · chain A against A, TM-score 1.00
P00730 · AlphaFold monomer V2.0 prediction for carboxypeptidase A1 (P00730) · 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 P00730
Elsewhere: RCSB PDB 5CPA · PDBe 5CPA · UniProt P00730

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