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4PYS

The crystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005764cellular_componentlysosome
A0005975biological_processcarbohydrate metabolic process
A0006689biological_processganglioside catabolic process
A0016020cellular_componentmembrane
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016787molecular_functionhydrolase activity
A0030203biological_processglycosaminoglycan metabolic process
A0046872molecular_functionmetal ion binding
A0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004563molecular_functionbeta-N-acetylhexosaminidase activity
B0005764cellular_componentlysosome
B0005975biological_processcarbohydrate metabolic process
B0006689biological_processganglioside catabolic process
B0016020cellular_componentmembrane
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016787molecular_functionhydrolase activity
B0030203biological_processglycosaminoglycan metabolic process
B0046872molecular_functionmetal ion binding
B0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
ACYS254
ACYS272
ACYS313
ACYS316

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
AASN478
AGLU480
AHOH774
AHOH792
BARG427
ATYR425
ATYR431
AGLU471
AHIS475
ASER476

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
AHIS241
AASP303
ATRP353
ATRP373
ATYR402
ATRP448
AGOL604
AHOH741

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 604
ChainResidue
AARG153
ATYR402
AASN404
ATRP448
AASP450
AGOL603
AFMT606
AHOH935
AHOH943

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 605
ChainResidue
AASP84
AARG93
AARG95
AGLU104
AHOH771
AHOH965
BARG95
BGLU104
BHOH810

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 606
ChainResidue
ATRP373
AASN398
APHE405
AARG417
AGOL604
AHOH873

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT A 607
ChainResidue
AGLY354
ATYR358
AGLN371
ATRP372
ATRP373
AASN374
AALA382
AHOH850

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 608
ChainResidue
ATYR399
ATYR400
ATHR418
AHOH830
AHOH931

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 609
ChainResidue
AILE22
AILE23
AILE30
ALYS488
AHOH930
AHOH974

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 610
ChainResidue
AASP483
AHOH969
BARG379
BASP380
BLYS384

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 601
ChainResidue
BCYS254
BCYS272
BCYS313
BCYS316

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 602
ChainResidue
BHIS241
BASP303
BTRP353
BTRP373
BTYR402
BGOL603
BHOH734
BHOH824
BHOH900

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 603
ChainResidue
BARG153
BTYR402
BASN404
BTRP448
BASP450
BGOL602
BFMT604
BHOH894
BHOH989

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT B 604
ChainResidue
BASN398
BPHE405
BARG417
BGOL603
BHOH906

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 605
ChainResidue
BGLN371
BTRP372
BTRP373
BASN374
BALA382
BGLY354
BTYR358

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FMT B 606
ChainResidue
BLYS163
BTYR164
BGLU455

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 607
ChainResidue
BGLY412
BTYR413
BTHR414
BARG417

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT B 608
ChainResidue
BSER146
BPHE147
BMSE148
BHIS177
BGLN371
BSER444
BSER445
BHOH957

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PDB entries from 2024-06-12

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