Structure of PDB 5a0x Chain A

Receptor sequence
>5a0xA (length=194) Species: 272563 (Clostridioides difficile 630) [Search protein sequence]
DSTTIQQNKDTLSQIVVFPTGNYDKNEANAMVNRLANIDGKYLNALKQNN
LKIKLLSGKLTDEKEYAYLKGVVPKGWEGTGKTWDDVPGLGGSTVALRIG
FSNKGKGHDAINLELHATAHAIDHIVLNDISKSAQFKQIFAKEGRSLGNV
NFLGVYPEEFFAESFAYYYLNQDTNSKLKSACPQTYSFLQNLAK
3D structure
PDB5a0x Structural Basis of Proline-Proline Peptide Bond Specificity of the Metalloprotease Zmp1 Implicated in Motility of Clostridium Difficile.
ChainA
Resolution1.7 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 A P100 K101 W103 W110 V113 L116 G117 G118 S119 H134 D135 A136 H142 H146 H150 N175 F178 E185 P74 K75 W77 W84 V87 L90 G91 G92 S93 H108 D109 A110 H116 H120 H124 N149 F152 E159
BS02 ZN A H142 H146 E185 H116 H120 E159
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:5a0x, PDBe:5a0x, PDBj:5a0x
PDBsum5a0x
PubMed26211609
UniProtQ183R7|PPEP1_CLOD6 Pro-Pro endopeptidase (Gene Name=zmp1)

[Back to BioLiP]