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4IRP

Crystal structure of catalytic domain of human beta1,4-galactosyltransferase-7 in open conformation with manganses and UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016757molecular_functionglycosyltransferase activity
B0005975biological_processcarbohydrate metabolic process
B0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE UDP A 401
ChainResidue
APRO100
AMN402
AHOH579
AHOH617
APHE101
AARG102
AARG104
APHE139
AASP163
AVAL164
AASP165
ATYR194

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AASP165
AHIS257
AUDP401
AHOH653

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 403
ChainResidue
AARG138
APHE139
AGLY223

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 404
ChainResidue
AASP79
APRO81
AARG117
AARG297

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 405
ChainResidue
AGLY91
APRO92
AHOH650
BALA88
BGLY91
BPRO92
BHOH637

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 406
ChainResidue
AASP174
AGLY176
APHE177

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD A 407
ChainResidue
APHE243
AHOH605
AHOH608
BHOH578

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UDP B 401
ChainResidue
BPRO100
BPHE101
BARG102
BARG104
BPHE139
BASP163
BVAL164
BASP165
BTYR194
BMN402
BHOH501

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN B 402
ChainResidue
BASP165
BHIS257
BUDP401
BHOH636

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 403
ChainResidue
BPRO92
BSER155

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 404
ChainResidue
BTRP84
BGLU85

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24052259","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IRP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IRQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24052259","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24052259","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IRQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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