MolNFT v1 · #124431 · protein

X-ray structure of a glucosamine N-acetyltransferase from clostridium acetobutylicum, apo form, pH 8

5KF2 · Predicted acetyltransferase: “X-ray structure of a glucosamine N-acetyltransferase from clostridium acetobutylicum, apo form, pH 8”. X-ray diffraction, 3 ligands (COA, ACO, PO4), 3 pockets (best druggability 0.68). MolNFT v1 #124431…

PDB: 5KF2
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Predicted acetyltransferase
UniProt: Q97ML2
Ligands: COA, ACO, PO4
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Predicted acetyltransferase	protein	317	36% helix, 32% strand	Q97ML2

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
ACO · Acetyl coenzyme *A · ligand · chains A
PO4 · Phosphate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 2 copies · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.68	0.96	22	empty
2	266	0.67	0.83	31	ACO, EDO
3	421	0.63	0.77	53	COA, PO4

Compared structures

5KF2 · X-ray structure of a glucosamine N-Acetyltransferase from Clostridium acetobutylicum, apo… · 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 Q97ML2
Elsewhere: RCSB PDB 5KF2 · PDBe 5KF2 · UniProt Q97ML2

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