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1CLC

THREE-DIMENSIONAL STRUCTURE OF ENDOGLUCANASE D AT 1.9 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008810molecular_functioncellulase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 650
ChainResidue
AGLU236
AASN239
AILE241
AASP243
AASP246
AHOH741

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 651
ChainResidue
AASP362
AASP401
AHOH677
AHOH730
ATHR356
ASER358
AASP361

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 652
ChainResidue
ASER520
AASP523
AILE525
AHOH668
AHOH686
AHOH856

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 653
ChainResidue
ACYS155
ACYS173
AHIS174
AHIS197

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DVNDDGKVNstDL
ChainResidueDetails
AASP585-LEU597
AASP621-VAL633

site_idPS00448
Number of Residues20
DetailsCLOS_CELLULOSOME_RPT Clostridium cellulosome enzymes repeated domain signature. DVNdDgkVNStDltlLkRyV
ChainResidueDetails
AASP585-VAL604
AASP621-LEU640

site_idPS00592
Number of Residues27
DetailsGH9_2 Glycosyl hydrolases family 9 (GH9) active site signature 2. HVFGrNyynrSYVTGl....GinPPmnPHDR
ChainResidueDetails
AHIS492-ARG518

site_idPS00698
Number of Residues19
DetailsGH9_3 Glycosyl hydrolases family 9 (GH9) active site signature 3. WvDiqdsYqtnEiAinwNA
ChainResidueDetails
ATRP544-ALA562

site_idPS60032
Number of Residues18
DetailsGH9_1 Glycosyl hydrolases family 9 (GH9) active site signature 1. StKGWHDAGDynKYvVNA
ChainResidueDetails
ASER192-ALA209

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10140
ChainResidueDetails
AGLY185

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10059, ECO:0000269|PubMed:2037583
ChainResidueDetails
AASN500

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10060, ECO:0000269|PubMed:1637316
ChainResidueDetails
APRO530

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10060, ECO:0000269|PubMed:1537833
ChainResidueDetails
APRO539

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1js4
ChainResidueDetails
AGLU555
AASP201
AASP198

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PDB entries from 2025-06-11

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