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3WUX

Crystal structure of unsaturated glucuronyl hydrolase mutant D115N/K370S from Streptococcus agalactiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0003824molecular_functioncatalytic activity
A0005975biological_processcarbohydrate metabolic process
A0009405biological_processobsolete pathogenesis
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0052757molecular_functionchondroitin hydrolase activity
A0102212molecular_functionunsaturated chondroitin disaccharide hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
ALEU319
ALYS320
ALYS329
AHOH519
AHOH526

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
AEDO406
AEDO406
AHOH515
AHOH555
ALYS320
ATYR321
AASP393
ATRP394

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
ATYR260
ALYS264
ATYR266
ALYS392
AASP393
AHOH542

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
AILE4
ALYS5
APRO6
AVAL7
AGLN267

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 405
ChainResidue
ATRP69
AGLN237
ATRP245
AARG247
ATRP251
AHOH582

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 406
ChainResidue
AEDO402
AEDO402
AHOH620
AHOH620

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 407
ChainResidue
ALEU19
AGLU330
ATYR334

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 408
ChainResidue
ATYR278
AARG282

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 409
ChainResidue
ALEU147
ACYS176
AASN179
AHIS202

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 410
ChainResidue
AHIS95
AASP133
ALYS135

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 411
ChainResidue
ATHR56
APHE57
AGLY369
ASER370
AGLY371
AHOH548

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 412
ChainResidue
AARG261
ALYS262
AHOH521

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:19416976
ChainResidueDetails
AASN115

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:19416976
ChainResidueDetails
AASP175

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AASN115
AASP175
AGLY233
ATHR235
AARG247
ATRP251
ASER365
ASER368

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PDB entries from 2024-10-30

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