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2JCK

Crystal structure of alpha-1,3 Galactosyltransferase (R365K) in complex with UDP and 2 manganese ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0016758molecular_functionhexosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A3362
ChainResidue
AASP1225
AASP1227
AHOH2406
AUDP3361

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A3363
ChainResidue
AGLN1247
AHIS1280
AGLU1317
AHOH2407

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE UDP A3361
ChainResidue
ALYS1104
APHE1134
AALA1135
AVAL1136
ATYR1139
AILE1198
ASER1199
AARG1202
AASP1225
AVAL1226
AASP1227
AGLU1360
AHOH2257
AHOH2403
AHOH2404
AHOH2405
AHOH2407
AMN3362
ALYS1102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:11179209, ECO:0007744|PDB:1G8O
ChainResidueDetails
AGLU1317

site_idSWS_FT_FI2
Number of Residues1
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
APHE1134

site_idSWS_FT_FI3
Number of Residues2
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
AASP1227
AASP1225

site_idSWS_FT_FI4
Number of Residues2
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
ATHR1259
AGLN1247

site_idSWS_FT_FI5
Number of Residues1
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
ALYS1359

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN1293

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 356
ChainResidueDetails
AGLN1247electrostatic stabiliser, hydrogen bond donor
AHIS1280electrostatic stabiliser, hydrogen bond donor
ATRP1314electrostatic stabiliser, hydrogen bond donor
AGLU1317activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
ATRP1356electrostatic stabiliser, hydrogen bond donor
ALYS1365electrostatic stabiliser

221051

PDB entries from 2024-06-12

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