Research workbench
Structure of a post-proline cleaving enzyme from rickettsia typhi
Analyse Structure of a post-proline cleaving enzyme from rickettsia typhi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HVT
- Type
- protein
- Length
- 691 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Post-proline cleaving enzyme
- EC
- 3.4.21.26
- UniProt
- Q68XJ3
- Ligands
- CL
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Post-proline cleaving enzyme (EC 3.4.21.26) | protein | 691 | 24% helix, 32% strand | Q68XJ3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1018 | 0.73 | 0.76 | 92 | CL |
| 2 | 878 | 0.72 | 0.77 | 75 | EDO |
| 3 | 70 | 0.43 | 0.81 | 18 | empty |
| 4 | 95 | 0.35 | 0.74 | 21 | EDO |
Compared structures
- 4HVT · Structure of a Post-proline cleaving enzyme from Rickettsia typhi · 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 Q68XJ3
- Elsewhere: RCSB PDB 4HVT · PDBe 4HVT · UniProt Q68XJ3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.