Research workbench
Crystal structure of the basic protease bprv from the ovine footrot pathogen, dichelobacter nodosus
Analyse Crystal structure of the basic protease bprv from the ovine footrot pathogen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TI7
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Basic extracellular subtilisin-like protease bprv
- EC
- 3.4.21.-
- UniProt
- A5EVD0
- Ligands
- CA
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Basic extracellular subtilisin-like protease bprv (EC 3.4.21.-) | protein | 340 | 29% helix, 18% strand | A5EVD0 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A
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 | 219 | 0.47 | 0.74 | 32 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3TI7 · Crystal structure of the basic protease BprV from the ovine footrot pathogen… · 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 A5EVD0
- Elsewhere: RCSB PDB 3TI7 · PDBe 3TI7 · UniProt A5EVD0
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