MolNFT v1 · #69421 · protein

Crystal structure of human ALPHA1-acid glycoprotein

3KQ0 · Alpha-1-acid glycoprotein 1: “Crystal structure of human ALPHA1-acid glycoprotein”. X-ray diffraction, 2 ligands (JIM, CL), 1 pocket (best druggability 0.72). MolNFT v1 #69421 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 3KQ0
Type: protein
Length: 175 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-1-acid glycoprotein 1
UniProt: P02763
Ligands: JIM, CL
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-1-acid glycoprotein 1	protein	175	26% helix, 41% strand	P02763

Ligands and binding sites

JIM · (2R)-2,3-dihydroxypropyl acetate · ligand · chains A
CL · Chloride ion · ion · 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	431	0.72	0.82	37	JIM

Modifications

Observed in the structure: 2 disulfide, 1 modified (disulfide, cyclization).

Compared structures

3KQ0 · Crystal structure of human alpha1-acid glycoprotein · the same entry in another collection · chain A against A, TM-score 1.00
P02763 · AlphaFold monomer V2.0 prediction for alpha-1-acid glycoprotein 1 (P02763) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P02763
Elsewhere: RCSB PDB 3KQ0 · PDBe 3KQ0 · UniProt P02763

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