Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KWS

CRYSTAL STRUCTURE OF BETA1,3-GLUCURONYLTRANSFERASE I IN COMPLEX WITH THE ACTIVE UDP-GLCUA DONOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0015018molecular_functiongalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
A0016020cellular_componentmembrane
B0015018molecular_functiongalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 500
ChainResidue
AASP196
AUGA404
AHOH501
AHOH502

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 501
ChainResidue
BASP196
BUGA405
BHOH502
BHOH503

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE UGA A 404
ChainResidue
ATHR83
ATYR84
AARG86
AASP113
AARG156
AGLY157
AARG161
AASP194
AASP195
AASP196
AASP252
AMET253
AHIS308
AARG310
AMN500
AHOH501
AHOH502
AHOH503
AHOH515
AHOH535
AHOH588
AHOH607
AHOH610
AHOH672
APRO82

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE UGA B 405
ChainResidue
BPRO82
BTHR83
BTYR84
BASP113
BPRO155
BARG156
BARG161
BASP194
BASP195
BASP196
BASP252
BMET253
BLEU280
BHIS308
BARG310
BMN501
BHOH502
BHOH503
BHOH506
BHOH511
BHOH517
BHOH598
BHOH622
BHOH647

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsRegion: {"description":"Interaction with galactose moiety of substrate glycoprotein"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues46
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"11950836","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Interaction with galactose moiety of substrate glycoprotein"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11950836
ChainResidueDetails
AGLU281

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11950836
ChainResidueDetails
BGLU281

site_idMCSA1
Number of Residues2
DetailsM-CSA 801
ChainResidueDetails
AASP196metal ligand
AGLU281proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 801
ChainResidueDetails
BASP196metal ligand
BGLU281proton acceptor, proton donor

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon