Structure of PDB 3c5m Chain B Binding Site BS01
Receptor Information
>3c5m Chain B (length=378) Species:
223926
(Vibrio parahaemolyticus RIMD 2210633) [
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AKGDVITLNFETFVDSDTQVKVTRLTPTDIICHRNYFYQKCFTQDGKKLL
FAGDFDGNRNYYLLNLETQQAVQLTEGKGDNTFGGFISTDERAFFYVKNE
LNLMKVDLETLEEQVIYTVDEEWKGYGTWVANSDCTKLVGIEILKRDWQP
LTSWEKFAEFYHTNPTCRLIKVDIETGELEVIHQDTAWLGHPIYRPFDDS
TVGFCHEGPHDLVDARMWLVNEDGSNVRKIKEHAEGESCTHEFWIPDGSA
MAYVSYFKGQTDRVIYKANPETLENEEVMVMPPCSHLMSNFDGSLMVGDG
CDAPVNIENDPFLYVLNTKAKSAQKLCKHSTSWDVLDGDRQITHPHPSFT
PNDDGVLFTSDFEGVPAIYIADVPESYK
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
3c5m Chain B Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
3c5m
Crystal structure of oligogalacturonate lyase (VPA0088) from Vibrio parahaemolyticus.
Resolution
2.6 Å
Binding residue
(original residue number in PDB)
H287 Q350 H353 H355
Binding residue
(residue number reindexed from 1)
H286 Q341 H344 H346
Annotation score
1
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0016829
lyase activity
GO:0046872
metal ion binding
GO:0047487
oligogalacturonide lyase activity
Biological Process
GO:0045490
pectin catabolic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:3c5m
,
PDBe:3c5m
,
PDBj:3c5m
PDBsum
3c5m
PubMed
UniProt
Q87K10
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