Research workbench
Human alanine aminotransferase 2 in complex with plp
Analyse Human alanine aminotransferase 2 in complex with plp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IHJ
- Type
- protein
- Length
- 461 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alanine aminotransferase 2
- EC
- 2.6.1.2
- UniProt
- Q8TD30
- Ligands
- PLP, PO4
- Pockets
- 7 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alanine aminotransferase 2 (EC 2.6.1.2) | protein | 461 | 47% helix, 18% strand | Q8TD30 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.55 | 0.76 | 32 | empty |
| 2 | 201 | 0.49 | 0.76 | 32 | empty |
| 3 | 94 | 0.45 | 0.79 | 23 | empty |
| 4 | 86 | 0.37 | 0.76 | 19 | empty |
| 5 | 69 | 0.32 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
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 Q8TD30
- Elsewhere: RCSB PDB 3IHJ · PDBe 3IHJ · UniProt Q8TD30
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