Research workbench
Refinement and comparison of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate
Analyse Refinement and comparison of the crystal structures of pig cytosolic aspartate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AJR
- Type
- protein
- Length
- 824 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- P00503
- Pockets
- 9 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 412 | 46% helix, 13% strand | P00503 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 617 | 0.70 | 0.78 | 71 | empty |
| 2 | 473 | 0.70 | 0.80 | 43 | empty |
| 3 | 103 | 0.69 | 0.92 | 28 | empty |
| 4 | 150 | 0.54 | 0.80 | 27 | empty |
| 5 | 110 | 0.53 | 0.82 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 3385 Ų buried · 64 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 1AJR · Refinement and comparison of the crystal structures of pig cytosolic aspartate… · the same entry in another collection · chain A against A, TM-score 1.00
- P00503 · AlphaFold monomer V2.0 prediction for aspartate aminotransferase, cytoplasmic (P00503) · a predicted model of the same protein · chain A 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 P00503
- Elsewhere: RCSB PDB 1AJR · PDBe 1AJR · UniProt P00503
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