Research workbench
Crystal structure of a putative peptidase T
Analyse Crystal structure of a putative peptidase T in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VIX
- Type
- protein
- Length
- 821 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidase T
- EC
- 3.4.11.14
- UniProt
- P29745
- Ligands
- ZN, SO4
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidase T (EC 3.4.11.14) | protein | 411 | 32% helix, 24% strand | P29745 |
| B | Peptidase T (EC 3.4.11.14) | protein | 410 | 34% helix, 23% strand | P29745 |
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 | 760 | 0.69 | 0.76 | 60 | ZN, SO4 |
| 2 | 797 | 0.69 | 0.76 | 61 | ZN, SO4 |
| 3 | 132 | 0.48 | 0.78 | 26 | empty |
| 4 | 125 | 0.47 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1339 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
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 P29745
- Elsewhere: RCSB PDB 1VIX · PDBe 1VIX · UniProt P29745
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