MolNFT v1 · #80383 · protein

Crystal structure of the humanized carboxyltransferase domain of yeast acetyl-CoA caroxylase in complex with compound 1

3TV5 · Acetyl-CoA carboxylase: “Crystal structure of the humanized carboxyltransferase domain of yeast acetyl-CoA caroxylase in complex with…”. X-ray diffraction, 1 ligand (RCP), 20 pockets (best druggability 0.85). MolNFT v1 #80383 on…

PDB: 3TV5
Type: protein
Length: 2,070 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA carboxylase
EC: 6.4.1.2, 6.3.4.14
UniProt: Q00955
Ligands: RCP
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 3 distinct chains · 40% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	696	40% helix, 20% strand	Q00955
B	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	690	41% helix, 21% strand	Q00955
C	Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14)	protein	684	41% helix, 21% strand	Q00955

Ligands and binding sites

RCP · (3R)-1'-(9-anthrylcarbonyl)-3-(morpholin-4-ylcarbonyl)-1,4'-bipiperidine · ligand · 3 copies · chains A, B, C

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1038	0.85	0.86	122	RCP
2	514	0.76	0.84	33	empty
3	288	0.72	0.85	37	RCP
4	534	0.71	0.80	34	empty
5	266	0.64	0.81	32	empty

Interfaces

2 interfaces between chains.

B–C · 5846 Å² buried · 50 hydrogen bonds · protein-protein
A–B · 1375 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

3TV5 · Crystal Structure of the humanized carboxyltransferase domain of yeast Acetyl-coA… · the same entry in another collection · chain A against A, TM-score 1.00
Q00955 · AlphaFold monomer V2.0 prediction for acetyl-CoA carboxylase (Q00955) · a predicted model of the same protein · chain C 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 Q00955
Elsewhere: RCSB PDB 3TV5 · PDBe 3TV5 · UniProt Q00955

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