Structure of PDB 2ewe Chain A

Receptor sequence
>2eweA (length=352) Species: 556 (Dickeya chrysanthemi) [Search protein sequence]
ATDTGGYAATAGGNVTGAVSKTATSMQDIVNIIDAARLDANGKKVKGGAY
PLVITYTGNEDSLINAAAANICGQWSKDPRGVEIKEFTKGITIIGANGSS
ANFGIWIKKSSDVVVQNMRIGYLPGGAKDGDMIRVDDSPNVWVDHNELFA
ANHECDGTPDNDTTFESAVDIKGASNTVTVSYNYIHGVKKVGLDGSSSSD
TGRNITYHHNYYNDVNAKLPLQRGGLVHAYNNLYTNITGSGLNVRQNGQA
LIENNWFEKAINPVTSRYDGKNFGTWVLKGNNITKPADFSTYSITWTADT
KPYVNADSWTSTGTFPTVAYNYSPVSAQCVKDKLPGYAGVGKNLATLTST
AC
3D structure
PDB2ewe Structure of a Plant Cell Wall Fragment Complexed to Pectate Lyase C
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D129 D131 A151 E166 D170 A217 K218 P220
Catalytic site (residue number reindexed from 1) D129 D131 A151 E166 D170 A217 K218 P220
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 ADA A D162 K218 R245 D162 K218 R245
BS02 ADA A D162 K190 L193 S196 R223 D162 K190 L193 S196 R223
BS03 ADA A K172 L193 K172 L193
BS04 CA A D129 D131 E166 D170 D129 D131 E166 D170
BS05 CA A D160 D162 D160 D162
BS06 CA A K218 Y268 K218 Y268
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0030570 pectate lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0045490 pectin catabolic process
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:2ewe, PDBe:2ewe, PDBj:2ewe
PDBsum2ewe
PubMed10368179
UniProtP11073|PLYC_DICCH Pectate lyase C (Gene Name=pelC)

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