Research workbench
X-ray crystal structure of L-azetidine-2-carboxylate hydrolase
Analyse X-ray crystal structure of L-azetidine-2-carboxylate hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SMV
- Type
- protein
- Length
- 233 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-(-)-azetidine-2-carboxylate hydrolase
- UniProt
- B2Z3V8
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-(-)-azetidine-2-carboxylate hydrolase | protein | 233 | 53% helix, 13% strand | B2Z3V8 |
Ligands and binding sites
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 | 427 | 0.73 | 0.83 | 44 | GOL |
Compared structures
- 3SMV · X-ray Crystal Structure of L-Azetidine-2-Carboxylate Hydrolase · 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 B2Z3V8
- Elsewhere: RCSB PDB 3SMV · PDBe 3SMV · UniProt B2Z3V8
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