MolNFT v1 · #191384 · protein

Cryo-EM structure of saccharomyces cerevisiae succinyl-COA:ACETATE CoA-transferase (ACH1P)

8DH7 · Acetyl-CoA hydrolase: “Cryo-EM structure of saccharomyces cerevisiae succinyl-COA:ACETATE CoA-transferase (ACH1P)”. Electron microscopy, 12 pockets (best druggability 0.73). MolNFT v1 #191384 on GenesisL1: 3D structure, binding…

PDB: 8DH7
Type: protein
Length: 1,052 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA hydrolase
EC: 3.1.2.1
UniProt: P32316
Pockets: 12 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 32% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Acetyl-CoA hydrolase (EC 3.1.2.1)	protein	526	32% helix, 20% strand	P32316

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	541	0.73	0.81	55	empty
2	56	0.72	0.99	22	empty
3	497	0.71	0.81	51	empty
4	107	0.62	0.88	27	empty
5	108	0.62	0.88	26	empty

Interfaces

1 interface between chains.

B–A · 3804 Å² buried · 46 hydrogen bonds · protein-protein

Compared structures

8DH7 · Cryo-EM structure of Saccharomyces cerevisiae Succinyl-CoA:acetate CoA-transferase (Ach1p) · the same entry in another collection · chain B against B, TM-score 1.00
P32316 · AlphaFold monomer V2.0 prediction for acetyl-CoA hydrolase (P32316) · a predicted model of the same protein · chain B 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 P32316
Elsewhere: RCSB PDB 8DH7 · PDBe 8DH7 · UniProt P32316

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