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Crystal structure of human GNA1

Analyse Crystal structure of human GNA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CXS
Type: protein
Length: 181 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucosamine 6-phosphate N-acetyltransferase
EC: 2.3.1.4
UniProt: Q96EK6
Pockets: 2 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucosamine 6-phosphate N-acetyltransferase (EC 2.3.1.4)	protein	181	35% helix, 23% strand	Q96EK6

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	126	0.45	0.77	21	empty
2	142	0.45	0.76	16	empty

Compared structures

3CXS · Crystal structure of human GNA1 · the same entry in another collection · chain A against A, TM-score 1.00
Q96EK6 · AlphaFold monomer V2.0 prediction for glucosamine 6-phosphate N-acetyltransferase (Q96EK6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q96EK6
Elsewhere: RCSB PDB 3CXS · PDBe 3CXS · UniProt Q96EK6

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