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1GWW

ALPHA-,1,3 GALACTOSYLTRANSFERASE - ALPHA-D-GLUCOSE COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0016758molecular_functionhexosyltransferase activity
B0005975biological_processcarbohydrate metabolic process
B0016020cellular_componentmembrane
B0016758molecular_functionhexosyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:11179209, ECO:0007744|PDB:1G8O
ChainResidueDetails
AGLU317
BGLU317

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ
ChainResidueDetails
APHE134
BPHE134

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1G8O, ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ
ChainResidueDetails
BASP225
BASP227
AASP225
AASP227

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2WGZ
ChainResidueDetails
BGLN247
BTHR259
AGLN247
ATHR259

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2WGZ
ChainResidueDetails
ALYS359
BLYS359

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN293
BASN293

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 356
ChainResidueDetails
AGLN247electrostatic stabiliser, hydrogen bond donor
AHIS280electrostatic stabiliser, hydrogen bond donor
ATRP314electrostatic stabiliser, hydrogen bond donor
AGLU317activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
ATRP356electrostatic stabiliser, hydrogen bond donor
AARG365electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 356
ChainResidueDetails
BGLN247electrostatic stabiliser, hydrogen bond donor
BHIS280electrostatic stabiliser, hydrogen bond donor
BTRP314electrostatic stabiliser, hydrogen bond donor
BGLU317activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
BTRP356electrostatic stabiliser, hydrogen bond donor
BARG365electrostatic stabiliser

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PDB entries from 2024-06-12

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