MolNFT v2 · #225969 · protein
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis in the holo form obtained at pH 7.0
8YRT · Aminotransferase class IV: “Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis in the holo form obtained at…”. X-ray diffraction at 2, 1 ligand (PLP), 1 pocket (best druggability 0.64). MolNFT v2 #225969…
- PDB
- 8YRT
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Haliscomenobacter hydrossis DSM 1100
- Molecule
- Aminotransferase class IV
- UniProt
- F4KWH0
- Ligands
- PLP
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminotransferase class IV | protein | 282 | 30% helix, 30% strand | F4KWH0 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.64 | 0.80 | 52 | PLP |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
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 F4KWH0
- Elsewhere: RCSB PDB 8YRT · PDBe 8YRT · UniProt F4KWH0
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