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2PEC

THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM

Replaces:  1PEC
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 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
Detailsa catalytic site defined by CSA, PubMed 10922032
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)

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PDB entries from 2025-07-30

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