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Crystal structure of the catalytic domain of corynebacterium mustelae predicted acetyltransferase acef (E2P).

Analyse Crystal structure of the catalytic domain of corynebacterium mustelae predicted… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZZM
Type: protein
Length: 475 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
EC: 2.3.1.-
UniProt: A0A0G3H170
Ligands: COA
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-)	protein	237	40% helix, 24% strand	A0A0G3H170
B	Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-)	protein	238	40% helix, 24% strand	A0A0G3H170

Ligands and binding sites

COA · Coenzyme A · ligand · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	410	0.63	0.77	55	COA
2	308	0.60	0.78	49	COA

Compared structures

6ZZM · Crystal structure of the catalytic domain of Corynebacterium mustelae predicted… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A0G3H170
Elsewhere: RCSB PDB 6ZZM · PDBe 6ZZM · UniProt A0A0G3H170 · AlphaFold DB A0A0G3H170

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