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1O0R

Crystal structure of the catalytic domain of bovine beta1,4-galactosyltransferase complex with UDP-galactose

Replaces:  1KYB
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 Residues27
DetailsBINDING SITE FOR RESIDUE GDU A 404
ChainResidue
APRO187
ALYS279
ATYR289
AGLY292
ATRP314
AGLY315
AGLU317
AMET344
AHIS347
AASP350
AMN403
APHE188
AHOH1005
AHOH1011
AHOH1050
AHOH1051
AHOH1069
AHOH1071
AHOH1178
AHOH1238
AARG189
AARG191
APHE226
AARG228
AASP252
AVAL253
AASP254

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GDU B 806
ChainResidue
BPRO187
BPHE188
BARG189
BARG191
BPHE226
BARG228
BASP252
BVAL253
BASP254
BLYS279
BGLY292
BTRP314
BGLY315
BGLU317
BASP318
BMET344
BHIS347
BASP350
BMN805
BHOH1036
BHOH1038
BHOH1091
BHOH1100
BHOH1105
BHOH1176
BHOH1231

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 805
ChainResidue
BASP254
BMET344
BHIS347
BGDU806
BHOH1002

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 403
ChainResidue
AASP254
AMET344
AHIS347
AGDU404
AHOH1011

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 901
ChainResidue
BALA221
BGLY222

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 902
ChainResidue
BARG265
BCYS266
BPHE267
BSER268
BHOH1182
BHOH1450

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 903
ChainResidue
AARG265
ACYS266
APHE267
ASER268
AHOH1402

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 904
ChainResidue
BHIS347
BSER348
BHOH1298
BHOH1344
BHOH1388
BHOH1424

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES A 900
ChainResidue
AALA221
AGLY222
AGLU223
ALEU383
AGLU384
ATHR395
AHOH1217
AHOH1375

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO A 905
ChainResidue
ALEU155
ATYR388
AHOH1052
AHOH1200

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DIO B 906
ChainResidue
BLEU155
BTYR391

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AASP260
BPHE327
BARG387
BPRO389
AGLN299
AALA326
APHE327
AARG387
APRO389
BASP260
BGLN299
BALA326

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:2117606
ChainResidueDetails
APRO163
BPRO163

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN190
BASN190

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 570
ChainResidueDetails
ALEU325electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
APHE327metal ligand
AARG387electrostatic stabiliser, hydrogen bond donor
ALEU390electrostatic stabiliser, hydrogen bond acceptor
ATYR391activator, electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 570
ChainResidueDetails
BLEU325electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BPHE327metal ligand
BARG387electrostatic stabiliser, hydrogen bond donor
BLEU390electrostatic stabiliser, hydrogen bond acceptor
BTYR391activator, electrostatic stabiliser, proton acceptor, proton donor

218853

PDB entries from 2024-04-24

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