Structure of PDB 1ru4 Chain A

Receptor sequence
>1ru4A (length=400) Species: 556 (Dickeya chrysanthemi) [Search protein sequence]
ADCSSDLTSGISTKRIYYVAPNGNSSNNGSSFNAPMSFSAAMAAVNPGEL
ILLKPGTYTIPYTQGKGNTITFNKSGKDGAPIYVAAANCGRAVFDFSFPD
SQWVQASYGFYVTGDYWYFKGVEVTRAGYQGAYVIGSHNTFENTAFHHNR
NTGLEINNGGSYNTVINSDAYRNYDPKKNGSMADGFGPKQKQGPGNRFVG
CRAWENSDDGFDLFDSPQKVVIENSWAFRNGINYWNDSAFAGNGNGFKLG
GNQAVGNHRITRSVAFGNVSKGFDQNNNAGGVTVINNTSYKNGINYGFGS
NVQSGQKHYFRNNVSLSASVTVSNADAKSNSWDTGPAASASDFVSLDTSL
ATVSRDNDGTLPETSLFRLSANSKLINAGTKESNISYSGSAPDLGAFERN
3D structure
PDB1ru4 The crystal structure of pectate lyase Pel9A from Erwinia chrysanthemi
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N268 K273
Catalytic site (residue number reindexed from 1) N243 K248
Enzyme Commision number 4.2.2.2: pectate lyase.
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 CA A D209 D233 D234 D237 D184 D208 D209 D212
BS02 CA A N402 S413 A416 D418 E423 N377 S388 A391 D393 E398
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0016837 carbon-oxygen lyase activity, acting on polysaccharides
GO:0030570 pectate lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0045490 pectin catabolic process
GO:0052009 symbiont-mediated disruption of host cell wall
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ru4, PDBe:1ru4, PDBj:1ru4
PDBsum1ru4
PubMed14670977
UniProtP0C1A7|PLYL_DICD3 Pectate lyase L (Gene Name=pelL)

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