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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABasic extracellular subtilisin-like protease bprv (EC 3.4.21.-)protein34029% helix, 18% strandA5EVD0

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12190.470.7432empty

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

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