MolNFT v1 · #53110 · protein

Biosynthetic thiolase from Z. ramigera. the N316H mutant.

2WKU · Acetyl-CoA acetyltransferase: “Biosynthetic thiolase from Z. ramigera. the N316H mutant.”. X-ray diffraction, 2 ligands (DNO, SO4), 16 pockets (best druggability 0.78). MolNFT v1 #53110 on GenesisL1: 3D structure, binding sites and…

PDB: 2WKU
Type: protein
Length: 1,556 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA acetyltransferase
EC: 2.3.1.9
UniProt: P07097
Ligands: DNO, SO4
Pockets: 16 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Acetyl-CoA acetyltransferase (EC 2.3.1.9)	protein	389	40% helix, 24% strand	P07097

Ligands and binding sites

DNO · D-mannose · ligand · 4 copies · chains A, B
SO4 · Sulfate ion · ion · 9 copies · chains A, B, C

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

Pockets

16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.78	0.98	40	empty
2	99	0.78	0.98	36	empty
3	143	0.61	0.84	30	empty
4	119	0.57	0.83	26	empty
5	115	0.56	0.84	26	empty

Interfaces

6 interfaces between chains.

C–D · 2670 Å² buried · 70 hydrogen bonds · protein-protein
A–B · 2658 Å² buried · 74 hydrogen bonds · protein-protein
B–C · 666 Å² buried · 12 hydrogen bonds · protein-protein
A–D · 634 Å² buried · 9 hydrogen bonds · protein-protein
B–D · 290 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2WKU · Biosynthetic thiolase from Z. ramigera. the N316H mutant. · the same entry in another collection · chain A against A, TM-score 1.00
P07097 · AlphaFold monomer V2.0 prediction for acetyl-CoA acetyltransferase (P07097) · 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 P07097
Elsewhere: RCSB PDB 2WKU · PDBe 2WKU · UniProt P07097

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