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1RU4

Crystal structure of pectate lyase Pel9A

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016829molecular_functionlyase activity
A0016837molecular_functioncarbon-oxygen lyase activity, acting on polysaccharides
A0030570molecular_functionpectate lyase activity
A0045490biological_processpectin catabolic process
A0046872molecular_functionmetal ion binding
A0052009biological_processsymbiont-mediated disruption of host cell wall
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1
ChainResidue
AASP209
AASP233
AASP234
AASP237
AHOH459
AHOH573

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 2
ChainResidue
AASP418
AGLU423
AHOH482
AASN402
ASER413
AALA416

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"14670977","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14670977","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RU4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 14670977
ChainResidueDetails
ALYS273
AASN268

site_idMCSA1
Number of Residues2
DetailsM-CSA 184
ChainResidueDetails
AASN268electrostatic stabiliser, hydrogen bond donor, increase acidity
ALYS273electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

238582

PDB entries from 2025-07-09

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