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GCN5-related N-acetyltransferase from kribbella flavida.

Analyse GCN5-related N-acetyltransferase from kribbella flavida. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IUS
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GCN5-related N-acetyltransferase
EC: 2.3.1.128
UniProt: D2PUG5
Ligands: SO4
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GCN5-related N-acetyltransferase (EC 2.3.1.128)	protein	257	32% helix, 30% strand	D2PUG5

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A
MLI · Malonate ion · additive · chains A

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

Pockets

3 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	96	0.72	0.95	33	empty
2	356	0.65	0.80	42	EDO
3	100	0.38	0.75	27	MLI

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

4IUS · GCN5-related N-acetyltransferase from Kribbella flavida. · 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 D2PUG5
Elsewhere: RCSB PDB 4IUS · PDBe 4IUS · UniProt D2PUG5

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