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3BMX

Beta-N-hexosaminidase (YbbD) from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 643
ChainResidue
AARG191
AHIS222
AHIS226
AHIS234
AASP318
AMET322

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 644
ChainResidue
ALYS477
AARG478
AGLN272
AILE290
ALEU291

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 645
ChainResidue
APRO274
APHE276
AASP277
AASP278
ALYS299

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 646
ChainResidue
AHIS226
ASER233
AALA269
AHIS270
AASP318

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 647
ChainResidue
AASP318
AMET322
AHOH696
AHOH942
AHOH1388

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 643
ChainResidue
BARG191
BHIS222
BHIS226
BSER233
BHIS234
BASP318
BMET322

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 644
ChainResidue
BPRO274
BALA275
BPHE276
BASP277
BASP278
BLYS299

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 645
ChainResidue
BASP230
BPRO238
BLEU239
BHOH870

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 646
ChainResidue
BILE90
BPHE92
BASP123
BMET267
BALA319
BLEU347

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 647
ChainResidue
BHIS226
BSER233
BALA269
BHIS270
BASP318

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 648
ChainResidue
BASP318
BMET322
BHOH780
BHOH1124

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE P4G A 648
ChainResidue
AASP34
ATYR399
APRO400
AASP530
ATHR531
AHOH1123
AHOH1377

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE P4G A 649
ChainResidue
AGLN244
AGLU245
AARG248
BTYR154
BTYR206

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE P4G B 649
ChainResidue
BTYR399
BTHR531
BHOH1009

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. LLRqEmgfnGVIVTDalN
ChainResidueDetails
ALEU304-ASN321

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:20826810, ECO:0000305|PubMed:23177201
ChainResidueDetails
AHIS234
BHIS234

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:20826810, ECO:0000305|PubMed:23177201
ChainResidueDetails
AASP318
BASP318

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20826810, ECO:0000269|PubMed:23177201
ChainResidueDetails
AASP123
AARG131
AARG191
ALYS221
BASP123
BARG131
BARG191
BLYS221

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000305|PubMed:20826810
ChainResidueDetails
AASP232
BASP232

site_idSWS_FT_FI5
Number of Residues2
DetailsLIPID: S-diacylglycerol cysteine => ECO:0000255|PROSITE-ProRule:PRU00303
ChainResidueDetails
ACYS17
BCYS17

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PDB entries from 2024-07-24

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