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6DHT

Bacteroides ovatus GH9 Bacova_02649

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008810molecular_functioncellulase activity
A0009279cellular_componentcell outer membrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033946molecular_functionxyloglucan-specific endo-beta-1,4-glucanase activity
A0085030biological_processsymbiotic process benefiting host
A2000899biological_processxyloglucan catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue IMD A 601
ChainResidue
AALA183
ATYR347
ATRP451
AGLU562
AALA564
ATRP567
APEG620

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 602
ChainResidue
AASP354
AGLU355
AGLY390
AHOH909
AASP349
AHIS351

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 603
ChainResidue
AGLU220
AASN223
ATHR225
AASP227
AASP230
AHOH999

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 604
ChainResidue
AGLU346
ATYR347
AHOH758
AHOH784
AHOH985

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 605
ChainResidue
APHE259
AHIS511
AARG513
AASP556
AHOH797
AHOH882

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 606
ChainResidue
AALA124
ALYS127
AILE216
AHOH825
AHOH870
AHOH886

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 607
ChainResidue
ASER212
AASN223
AHIS224
ATHR225
APRO226

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO A 608
ChainResidue
AGLN205
AARG294
ALEU295
AHOH735
AHOH934

site_idAC9
Number of Residues2
Detailsbinding site for residue EDO A 609
ChainResidue
ATYR364
AHOH863

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO A 610
ChainResidue
AGLU370
AARG373
AGLU374

site_idAD2
Number of Residues7
Detailsbinding site for residue EDO A 611
ChainResidue
ALEU401
AARG412
AALA415
AASP416
AGLN471
AHOH824
AHOH837

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO A 612
ChainResidue
APRO381
AGLN382
ASER417
AGLU421

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO A 613
ChainResidue
AASP475
ALEU478
ATHR479
AEDO614
AHOH905

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO A 614
ChainResidue
AGLN43
ATYR482
AALA582
AEDO613
AHOH1022

site_idAD6
Number of Residues2
Detailsbinding site for residue EDO A 615
ChainResidue
ALEU206
APHE207

site_idAD7
Number of Residues5
Detailsbinding site for residue EDO A 616
ChainResidue
ALEU407
AASN408
AGLU409
AARG412
AHOH741

site_idAD8
Number of Residues2
Detailsbinding site for residue EDO A 617
ChainResidue
AARG213
AHOH873

site_idAD9
Number of Residues7
Detailsbinding site for residue PEG A 618
ChainResidue
ATYR425
AGLU456
ALYS457
AGLN461
ACL621
AHOH826
AHOH1118

site_idAE1
Number of Residues2
Detailsbinding site for residue PEG A 619
ChainResidue
AASN533
AHOH784

site_idAE2
Number of Residues9
Detailsbinding site for residue PEG A 620
ChainResidue
AGLY388
ATRP389
ATRP451
AGLU456
AASN566
ATRP567
AIMD601
AHOH894
AHOH1024

site_idAE3
Number of Residues5
Detailsbinding site for residue CL A 621
ChainResidue
ATHR385
AALA386
APEG618
AHOH1118
AHOH1176

site_idAE4
Number of Residues4
Detailsbinding site for residue CL A 622
ChainResidue
AASP185
ATYR186
AASN187
AGLU260

site_idAE5
Number of Residues6
Detailsbinding site for residue MG A 623
ChainResidue
ASER515
AASP518
AILE520
AHOH811
AHOH942
AHOH951

Functional Information from PROSITE/UniProt
site_idPS00592
Number of Residues27
DetailsGH9_2 Glycosyl hydrolases family 9 (GH9) active site signature 2. YILGrNatgfCYVTGl....GtkSPkhPHHR
ChainResidueDetails
ATYR487-ARG513

site_idPS00698
Number of Residues19
DetailsGH9_3 Glycosyl hydrolases family 9 (GH9) active site signature 3. YvDtedsYasnEvAinwNA
ChainResidueDetails
ATYR551-ALA569

site_idPS60032
Number of Residues18
DetailsGH9_1 Glycosyl hydrolases family 9 (GH9) active site signature 1. SsKGWYDAGDynKYiVNS
ChainResidueDetails
ASER176-SER193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10140","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10060","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10060","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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