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1GQ8

Pectin methylesterase from Carrot

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0030599molecular_functionpectinesterase activity
A0042545biological_processcell wall modification
A0045490biological_processpectin catabolic process
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CAC A 501
ChainResidue
AGLN135
AASP136
AASP157
AHOH2345

site_idAC2
Number of Residues5
Detailsbinding site for residue CAC A 502
ChainResidue
ASER217
AGLY299
AHOH2080
AHOH2179
AHOH2180

Functional Information from PROSITE/UniProt
site_idPS00503
Number of Residues10
DetailsPECTINESTERASE_2 Pectinesterase signature 2. IaGTVDFIFG
ChainResidueDetails
AILE152-GLY161

site_idPS00800
Number of Residues20
DetailsPECTINESTERASE_1 Pectinesterase signature 1. SktryviRIKaGVYREnvdV
ChainResidueDetails
ASER33-VAL52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 11943159
ChainResidueDetails
AASP136
AGLN113
AGLN135
AASP157

site_idMCSA1
Number of Residues5
DetailsM-CSA 681
ChainResidueDetails
ALEU117electrostatic stabiliser
ATYR139electrostatic stabiliser
AVAL140increase nucleophilicity, proton acceptor, proton donor
AGLY161covalently attached, nucleofuge, nucleophile
AGLU229electrostatic stabiliser

250059

PDB entries from 2026-03-04

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