Structure of PDB 3d3x Chain B

Receptor sequence
>3d3xB (length=407) Species: 1492 (Clostridium butyricum) [Search protein sequence]
PKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWIIPERNVIGTT
PQDFHPPTKNGDSSYYDPNYLQSDEEKDRFLKIVTKIFNRINNNLSGGIL
LEELSKANPYLGNDNTPDNQFHIGDASAVEIKFSNGSQDILLPNVIIMGA
EPDLFETNSSNISLRNNYMPSNHGFGSIAIVTFSPEYSFRFNDNSMNEFI
QDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLITNIRGTNIEEFL
TFGGTDLNIITSAQSNDIYTNLLADYKKIASKLSKVQVSNPLLNPYKDVF
EAKYGLDKDASGIYSVNINKFNDIFKKLYSFTEFDLATKFQVKCRQTYIG
QYKYFKLSNLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITGRG
LVKKIIR
3D structure
PDB3d3x SNAP-25 substrate peptide (residues 180-183) binds to but bypasses cleavage by catalytically active Clostridium botulinum neurotoxin E.
ChainB
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H211 E212 H215 E250 R347
Catalytic site (residue number reindexed from 1) H209 E210 H213 E248 R345
Enzyme Commision number ?
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 E158 T159 N160 T208 H211 E212 N242 T246 R347 Y350 Q353 Y356 E156 T157 N158 T206 H209 E210 N240 T244 R345 Y348 Q351 Y354
BS02 ZN B H211 H215 E250 H209 H213 E248
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:3d3x, PDBe:3d3x, PDBj:3d3x
PDBsum3d3x
PubMed18658150
UniProtQ9K395

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