MolNFT v1 · #68431 · protein

Crystal structure of the acetyltransferase VF_1542 from vibrio fischeri, northeast structural genomics consortium target VFR136

3JVN: “Crystal structure of the acetyltransferase VF_1542 from vibrio fischeri, northeast structural genomics…”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.43). MolNFT v1 #68431 on GenesisL1: 3D structure, binding…

PDB: 3JVN
Type: protein
Length: 122 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyltransferase
EC: 2.3.1.-
UniProt: Q5E4K9
Ligands: SO4
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyltransferase (EC 2.3.1.-)	protein	122	34% helix, 32% strand	Q5E4K9

Ligands and binding sites

SO4 · Sulfate 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	133	0.43	0.76	19	empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

3JVN · Crystal Structure of the acetyltransferase VF_1542 from Vibrio fischeri, Northeast… · 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 Q5E4K9
Elsewhere: RCSB PDB 3JVN · PDBe 3JVN · UniProt Q5E4K9

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