MolNFT v1 · #135180 · protein
Crystal structure of phosphorylated AC3-AC5 domains of yeast acetyl- CoA carboxylase
5TRC · Acetyl-CoA carboxylase: “Crystal structure of phosphorylated AC3-AC5 domains of yeast acetyl- CoA carboxylase”. X-ray diffraction, 1 ligand (CL), 12 pockets (best druggability 0.69). MolNFT v1 #135180 on GenesisL1: 3D structure…
- PDB
- 5TRC
- Type
- protein
- Length
- 824 residues
- Chains
- 2
- 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
- CL
- Pockets
- 12 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 426 | 31% helix, 26% strand | Q00955 |
| B | Acetyl-CoA carboxylase (EC 6.4.1.2, 6.3.4.14) | protein | 398 | 33% helix, 28% strand | Q00955 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 542 | 0.69 | 0.79 | 58 | empty |
| 2 | 295 | 0.64 | 0.81 | 35 | CL |
| 3 | 455 | 0.63 | 0.76 | 57 | CL |
| 4 | 206 | 0.59 | 0.81 | 24 | empty |
| 5 | 182 | 0.56 | 0.80 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 937 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 5TRC · Crystal structure of phosphorylated AC3-AC5 domains of yeast acetyl-CoA carboxylase · 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 B against A, TM-score 0.87
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 5TRC · PDBe 5TRC · UniProt Q00955
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