Research workbench
Crystal structure of the tetrahedral aminopeptidase from P. horikoshii
Analyse Crystal structure of the tetrahedral aminopeptidase from P. horikoshii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y0R
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Frv operon protein frvx
- UniProt
- O59196
- Ligands
- ZN, ARS
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Frv operon protein frvx | protein | 333 | 31% helix, 31% strand | O59196 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.38 | 0.77 | 20 | ARS |
Compared structures
- 1Y0R · Crystal structure of the tetrahedral aminopeptidase from P. horikoshii · the same entry in another collection · chain A against A, TM-score 1.00
- O59196 · AlphaFold monomer V2.0 prediction for tetrahedral aminopeptidase (O59196) · a predicted model of the same protein · 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 O59196
- Elsewhere: RCSB PDB 1Y0R · PDBe 1Y0R · UniProt O59196
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