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Structure of acetyl-CoA acetyltransferase from syntrophomonas wolfei

Analyse Structure of acetyl-CoA acetyltransferase from syntrophomonas wolfei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7N7Z
Type: protein
Length: 795 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA C-acetyltransferase
EC: 2.3.1.9
UniProt: Q0AZ52
Pockets: 5 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA C-acetyltransferase (EC 2.3.1.9)	protein	396	41% helix, 22% strand	Q0AZ52
B	Acetyl-CoA C-acetyltransferase (EC 2.3.1.9)	protein	399	39% helix, 21% strand	Q0AZ52

Pockets

5 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	123	0.64	0.87	38	empty
2	122	0.58	0.84	33	empty
3	56	0.51	0.88	16	empty
4	123	0.41	0.75	22	empty
5	104	0.36	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 2785 Å² buried · 74 hydrogen bonds · protein-protein

Compared structures

7N7Z · Structure of Acetyl-CoA acetyltransferase from Syntrophomonas wolfei · 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 Q0AZ52
Elsewhere: RCSB PDB 7N7Z · PDBe 7N7Z · UniProt Q0AZ52

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