Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4C2L

Crystal structure of endo-xylogalacturonan hydrolase from Aspergillus tubingensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004650molecular_functionpolygalacturonase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0045490biological_processpectin catabolic process
A0071555biological_processcell wall organization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsRepeat: {"description":"PbH1 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues43
DetailsRepeat: {"description":"PbH1 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues23
DetailsRepeat: {"description":"PbH1 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsRepeat: {"description":"PbH1 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues42
DetailsRepeat: {"description":"PbH1 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon