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4CJ0

Crystal structure of CelD in complex with affitin E12

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 Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1576
ChainResidue
ATHR356
ASER358
AASP361
AASP362
AASP401
AHOH2602
AHOH2603

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1577
ChainResidue
AILE241
AASP243
AASP246
AHOH2458
AGLU236
AASN239

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1578
ChainResidue
ASER520
AASP523
AILE525
AHOH2776
AHOH2777
AHOH2778
AHOH2779

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1579
ChainResidue
ACYS155
ACYS173
AHIS174
AHIS197

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 1067
ChainResidue
AASP397
ATYR456
AHOH2653
BARG25
BASN26
BLEU27
BHOH2011
BHOH2041
BHOH2042

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1580
ChainResidue
ALEU335
AARG363
AASP382
AARG386
AHOH2566
AHOH2607
AHOH2819

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 1581
ChainResidue
APRO172
ACYS173
AHIS174
ATHR175
APRO282
AGLU283
AGLU285
AHIS286
AHOH2331
AHOH2820

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1068
ChainResidue
APHE276
ATYR551
BTYR30
BHOH2043
BHOH2044

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1582
ChainResidue
AASP201
APHE276
AHIS516
AARG518
ATYR551
AGLU555
AHOH2821
BLYS29
BTYR30

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1583
ChainResidue
AASP399
ATRP400
AASP401
ATYR456
AHOH2648
AHOH2658
AHOH2720
BLEU27

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
AASP201

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

223532

PDB entries from 2024-08-07

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