MolNFT v1 · #66816 · protein

Carboxypeptidase a inhibited by a thiirane mechanism-based inactivator

3I1U · Carboxypeptidase A1 (pancreatic): “Carboxypeptidase a inhibited by a thiirane mechanism-based inactivator”. X-ray diffraction, 2 ligands (BTW, ZN), 1 pocket (best druggability 0.63). MolNFT v1 #66816 on GenesisL1: 3D structure…

PDB: 3I1U
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxypeptidase A1 (pancreatic)
EC: 3.4.17.1
UniProt: A6H6Y4
Ligands: BTW, ZN
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxypeptidase A1 (pancreatic) (EC 3.4.17.1)	protein	303	40% helix, 18% strand	A6H6Y4

Ligands and binding sites

BTW · (2S,3R)-2-benzyl-3-sulfanylbutanoic acid · ligand · chains A
ZN · Zinc ion · metal · chains A
GOL · Glycerol · additive · 7 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	81	0.63	0.90	24	BTW

Modifications

Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

3I1U · Carboxypeptidase A Inhibited by a Thiirane Mechanism-Based inactivator · 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 A6H6Y4
Elsewhere: RCSB PDB 3I1U · PDBe 3I1U · UniProt A6H6Y4

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