MolNFT v1 · #1128 · protein

GDP+PI bound G42V GIA1

1AS2: “GDP+PI bound G42V GIA1”. X-ray diffraction, 2 ligands (GDP, PO4), 4 pockets (best druggability 0.74). MolNFT v1 #1128 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1AS2
Type: protein
Length: 315 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GIA1
UniProt: P10824
Ligands: GDP, PO4
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GIA1	protein	315	51% helix, 13% strand	P10824

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
PO4 · Phosphate ion · ion · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	193	0.74	0.90	35	PO4, GDP
2	224	0.59	0.80	28	empty
3	120	0.47	0.78	26	empty
4	63	0.33	0.76	13	empty

Compared structures

1AS2 · GDP+PI bound G42V GIA1 · the same entry in another collection · chain A against A, TM-score 1.00
P10824 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I) subunit… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P10824
Elsewhere: RCSB PDB 1AS2 · PDBe 1AS2 · UniProt P10824

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