MolNFT v1 · #7626 · protein
Thermus thermophilus aspartate aminotransferase tetra mutant 2 complexed with tryptophan
1GC3: “Thermus thermophilus aspartate aminotransferase tetra mutant 2 complexed with tryptophan”. X-ray diffraction, 2 ligands (TRP, PLP), 20 pockets (best druggability 0.79). MolNFT v1 #7626 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1GC3
- Type
- protein
- Length
- 3,056 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- Q56232
- Ligands
- TRP, PLP
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Aspartate aminotransferase (EC 2.6.1.1) | protein | 382 | 43% helix, 14% strand | Q56232 |
Ligands and binding sites
- TRP · Tryptophan · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- PLP · Pyridoxal-5'-phosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.79 | 0.88 | 53 | TRP, PLP |
| 2 | 447 | 0.77 | 0.85 | 55 | TRP, PLP |
| 3 | 445 | 0.77 | 0.86 | 61 | TRP, PLP |
| 4 | 633 | 0.76 | 0.82 | 72 | TRP, PLP |
| 5 | 508 | 0.75 | 0.83 | 67 | TRP, PLP |
Interfaces
8 interfaces between chains.
- E–F · 3172 Ų buried · 62 hydrogen bonds · protein-protein
- C–D · 3128 Ų buried · 66 hydrogen bonds · protein-protein
- G–H · 3113 Ų buried · 64 hydrogen bonds · protein-protein
- A–B · 3097 Ų buried · 64 hydrogen bonds · protein-protein
- B–D · 386 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1GC3 · Thermus thermophilus aspartate aminotransferase tetra mutant 2 complexed with tryptophan · the same entry in another collection · chain G against G, TM-score 1.00
- Q56232 · AlphaFold monomer V2.0 prediction for ASPARTATE/PREPHENATE aminotransferase (Q56232) · a predicted model of the same protein · chain H 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 Q56232
- Elsewhere: RCSB PDB 1GC3 · PDBe 1GC3 · UniProt Q56232
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