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Crystal structure of human acaca C-terminal domain
Analyse Crystal structure of human acaca C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ASI
- Type
- protein
- Length
- 4,428 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA carboxylase 1
- EC
- 6.4.1.2, 6.3.4.14
- UniProt
- Q13085
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 6 distinct chains · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 751 | 47% helix, 19% strand | Q13085 |
| B | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 738 | 46% helix, 20% strand | Q13085 |
| C | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 755 | 47% helix, 19% strand | Q13085 |
| D | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 745 | 47% helix, 19% strand | Q13085 |
| E | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 721 | 45% helix, 20% strand | Q13085 |
| F | Acetyl-CoA carboxylase 1 (EC 6.4.1.2, 6.3.4.14) | protein | 718 | 45% helix, 20% strand | Q13085 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 873 | 0.83 | 0.85 | 86 | empty |
| 2 | 1182 | 0.82 | 0.83 | 108 | empty |
| 3 | 724 | 0.80 | 0.83 | 63 | empty |
| 4 | 401 | 0.73 | 0.83 | 50 | empty |
| 5 | 297 | 0.72 | 0.85 | 44 | empty |
Interfaces
5 interfaces between chains.
- A–C · 7759 Ų buried · 62 hydrogen bonds · protein-protein
- B–D · 6939 Ų buried · 54 hydrogen bonds · protein-protein
- E–F · 6035 Ų buried · 48 hydrogen bonds · protein-protein
- A–B · 924 Ų buried · 26 hydrogen bonds · protein-protein
- D–E · 265 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 Q13085
- Elsewhere: RCSB PDB 4ASI · PDBe 4ASI · UniProt Q13085
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