Research workbench
Crystal structure of D-serine dehydratase in complex with D-serine from chicken kidney (edta-treated)
Analyse Crystal structure of D-serine dehydratase in complex with D-serine from chicken… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AWO
- Type
- protein
- Length
- 368 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-serine dehydratase
- EC
- 4.3.1.18
- UniProt
- A9CP13
- Ligands
- PLP, DSN
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-serine dehydratase (EC 4.3.1.18) | protein | 368 | 37% helix, 25% strand | A9CP13 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.55 | 0.79 | 40 | PLP, DSN |
| 2 | 60 | 0.28 | 0.74 | 21 | empty |
Compared structures
- 3AWO · Crystal structure of D-serine dehydratase in complex with D-serine from chicken kidney… · 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
- Every structure of UniProt A9CP13
- Elsewhere: RCSB PDB 3AWO · PDBe 3AWO · UniProt A9CP13
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