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1V83

Crystal structure of human GlcAT-P in complex with Udp and Mn2+

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 501
ChainResidue
AASP197
AUDP503
AHOH504
AHOH505

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 502
ChainResidue
BASP197
BUDP504
BHOH505
BHOH506

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TLA A 500
ChainResidue
AARG240
ATRP241
AHIS248
AHOH618
AHOH636
BARG213
BARG263
BGLN267
AARG231

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UDP A 503
ChainResidue
APRO91
ATHR92
ATYR93
AASP122
ALYS153
AARG165
AGLY166
AARG170
AASP195
AASP196
AASP197
AHIS311
AARG313
AMN501
AHOH584

site_idAC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE UDP B 504
ChainResidue
BPRO91
BTHR92
BTYR93
BASP122
BARG165
BGLY166
BASP195
BASP196
BASP197
BHIS311
BARG313
BMN502
BHOH591
BHOH611
BHOH681
BHOH725

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsRegion: {"description":"Interaction with galactose moiety of substrate glycoprotein"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Interaction with galactose moiety of substrate glycoprotein"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Interaction with galactose moiety of substrate glycoprotein","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"O35789","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kws
ChainResidueDetails
AGLU284

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kws
ChainResidueDetails
BGLU284

242500

PDB entries from 2025-10-01

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