Research workbench
Human MAK3 homolog in complex with acetyl-CoA
Analyse Human MAK3 homolog in complex with acetyl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OB0
- Type
- protein
- Length
- 472 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human MAK3 homolog
- EC
- 2.3.1.88
- UniProt
- Q9GZZ1
- Ligands
- ACO
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human MAK3 homolog (EC 2.3.1.88) | protein | 154 | 32% helix, 36% strand | Q9GZZ1 |
| B | Human MAK3 homolog (EC 2.3.1.88) | protein | 152 | 32% helix, 34% strand | Q9GZZ1 |
| C | Human MAK3 homolog (EC 2.3.1.88) | protein | 166 | 31% helix, 33% strand | Q9GZZ1 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.68 | 0.81 | 43 | ACO |
| 2 | 337 | 0.68 | 0.82 | 35 | ACO |
| 3 | 374 | 0.67 | 0.80 | 41 | ACO |
| 4 | 378 | 0.66 | 0.80 | 46 | empty |
| 5 | 186 | 0.50 | 0.78 | 23 | empty |
Interfaces
2 interfaces between chains.
- A–C · 630 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 443 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
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 Q9GZZ1
- Elsewhere: RCSB PDB 2OB0 · PDBe 2OB0 · UniProt Q9GZZ1
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