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4CJ1

Crystal structure of CelD in complex with affitin H3

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008810molecular_functioncellulase activity
B0003677molecular_functionDNA binding
B0004521molecular_functionRNA endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1578
ChainResidue
ACYS155
ACYS173
AHIS174
AHIS197

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1579
ChainResidue
AHOH2382
AGLU236
AASN239
AILE241
AASP243
AASP246

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1580
ChainResidue
ATHR356
ASER358
AASP361
AASP362
AASP401
AHOH2522
AHOH2523

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1581
ChainResidue
ASER520
AASP523
AILE525
AHOH2706
AHOH2707
AHOH2708
AHOH2709

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1582
ChainResidue
APHE223
AGLN226
AGLN471
AASN474
AVAL483
AGLY570
APHE571
AHOH2661
AHOH2666

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1583
ChainResidue
AASP201
AHIS516
AARG518
AGLU555
BARG29

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1584
ChainResidue
AGLU140
AASN573
ATYR574
AHOH2181
AHOH2184
AHOH2189
AHOH2745
AHOH2747

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1585
ChainResidue
APRO172
ACYS173
AHIS174
ATHR175
APRO282
AGLU283
AGLU285
AHIS286
AHOH2277

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 Residues2
DetailsMOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:3130377
ChainResidueDetails
BLYS5
BHIS7

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10059, ECO:0000269|PubMed:2037583
ChainResidueDetails
AHIS516

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10060, ECO:0000269|PubMed:1637316
ChainResidueDetails
AASP546

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10060, ECO:0000269|PubMed:1537833
ChainResidueDetails
AGLU555

220113

PDB entries from 2024-05-22

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