Structure of PDB 5a0r Chain B

Receptor sequence
>5a0rB (length=192) Species: 272563 (Clostridioides difficile 630) [Search protein sequence]
TTIQQNKDTLSQIVVFPTGNYDKNEANAMVNRLANIDGKYLNALKQNNLK
IKLLSGKLTDEKEYAYLKGVVPKGWEGTGKTWDDVPGLGGSTVALRIGFS
NKGKGHDAINLELHATAHAIDHIVLNDISKSAQFKQIFAKEGRSLGNVNY
LGVYPEEFFAESFAYYYLNQDTNSKLKSACPQTYSFLQNLAK
3D structure
PDB5a0r Structural Basis of Proline-Proline Peptide Bond Specificity of the Metalloprotease Zmp1 Implicated in Motility of Clostridium Difficile.
ChainB
Resolution1.251 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.4.24.89: Pro-Pro endopeptidase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 peptide B W110 L116 G117 G118 S119 H142 H146 Y178 E185 W82 L88 G89 G90 S91 H114 H118 Y150 E157
BS02 ZN B H142 H146 E185 H114 H118 E157
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:5a0r, PDBe:5a0r, PDBj:5a0r
PDBsum5a0r
PubMed26211609
UniProtQ183R7|PPEP1_CLOD6 Pro-Pro endopeptidase (Gene Name=zmp1)

[Back to BioLiP]