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1O8H

Pectate Lyase C from Erwinia Chrysanthemi at pH 9.5 with 0.3mM Ca2+ Added

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016829molecular_functionlyase activity
A0030570molecular_functionpectate lyase activity
A0045490biological_processpectin catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A1353
ChainResidue
AASP129
AASP131
AGLU166
AASP170
AHOH2113
AHOH2115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12540845","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2pec
ChainResidueDetails
AASP131
AARG218

site_idMCSA1
Number of Residues5
DetailsM-CSA 896
ChainResidueDetails
AASP129metal ligand
AASP131metal ligand
AGLU166metal ligand
AASP170metal ligand
AARG218modifies pKa, proton shuttle (general acid/base)

238582

PDB entries from 2025-07-09

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