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Crystal structure of a gnat superfamily acetyltransferase PA4794 in complex with hepes

Analyse Crystal structure of a gnat superfamily acetyltransferase PA4794 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4M3S
Type: protein
Length: 160 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q9HV14
Ligands: CL, SO4
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	160	34% helix, 37% strand	Q9HV14

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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	308	0.65	0.81	37	CL, EPE

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

4M3S · Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with HEPES · 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 Q9HV14
Elsewhere: RCSB PDB 4M3S · PDBe 4M3S · UniProt Q9HV14

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