Structure of PDB 5bqm Chain A

Receptor sequence
>5bqmA (length=442) Species: 1491 (Clostridium botulinum) [Search protein sequence]
TWPVKDFNYSDPVNDNDILYLRIPQNKLITTPVKAFMITQNIWVIPERFS
SDTNPSLSKPPRPTSKYQSYYDPSYLSTDEQKDTFLKGIIKLFKRINERD
IGKKLINYLVVGSPFMGDSSTPEDTFDFTRHTTNIAVEKFENGSWKVTNI
ITPSVLIFGPLPNILDYTASLTLQGQQSNPSFEGFGTLSILKVAPEFLLT
FSDVTSNQSSAVLGKSIFCMDPVIALMHELTHSLHQLYGINIPSDKRIRP
QVSEGFFSQDGPNVQFEELYTFGGLDVEIIPQIERSQLREKALGHYKDIA
KRLNNINKTIPSSWISNIDKYKKIFSEKYNFDKDNTGNFVVNIDKFNSLY
SDLTNVMSEVVYSSQYNVKNRTHYFSRHYLPVFANILDDNIYTIRDGFNL
TNKGFNIENSGQNIERNPALQKLSSESVVDLFTKVCVDGIIT
3D structure
PDB5bqm Structural analysis of Clostridium botulinum neurotoxin type D as a platform for the development of targeted secretion inhibitors.
ChainA
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H229 E230 H233 E269 R372
Catalytic site (residue number reindexed from 1) H228 E229 H232 E268 R371
Enzyme Commision number 3.4.24.69: bontoxilysin.
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 ZN A H229 H233 E269 H228 H232 E268
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5bqm, PDBe:5bqm, PDBj:5bqm
PDBsum5bqm
PubMed26324071
UniProtP19321|BXD_CBDP Botulinum neurotoxin type D (Gene Name=botD)

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