Research workbench
Crystal structure of aspartate aminotransferase (TM1698) from thermotoga maritima at 2.50 a resolution
Analyse Crystal structure of aspartate aminotransferase (TM1698) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GB3
- Type
- protein
- Length
- 2,346 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 6 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase | protein | 389 | 43% helix, 16% strand | — |
| B | Aspartate aminotransferase | protein | 394 | 43% helix, 16% strand | — |
| C | Aspartate aminotransferase | protein | 391 | 44% helix, 16% strand | — |
| D | Aspartate aminotransferase | protein | 390 | 43% helix, 16% strand | — |
| E | Aspartate aminotransferase | protein | 393 | 44% helix, 16% strand | — |
| F | Aspartate aminotransferase | protein | 389 | 43% helix, 16% strand | — |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 956 | 0.79 | 0.81 | 72 | empty |
| 2 | 608 | 0.77 | 0.83 | 55 | empty |
| 3 | 514 | 0.75 | 0.83 | 52 | empty |
| 4 | 552 | 0.74 | 0.82 | 57 | empty |
| 5 | 82 | 0.74 | 0.97 | 24 | empty |
Interfaces
7 interfaces between chains.
- E–F · 2973 Ų buried · 57 hydrogen bonds · protein-protein
- A–B · 2957 Ų buried · 60 hydrogen bonds · protein-protein
- C–D · 2934 Ų buried · 53 hydrogen bonds · protein-protein
- B–F · 580 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 217 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 63 modified (engineered, cofactor).
Compared structures
- 2GB3 · Crystal structure of Aspartate aminotransferase (tm1698) from Thermotoga maritima at 2.50… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 2GB3 · PDBe 2GB3
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