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3ITK

Crystal structure of human UDP-glucose dehydrogenase Thr131Ala, apo form.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001702biological_processgastrulation with mouth forming second
A0003979molecular_functionUDP-glucose 6-dehydrogenase activity
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006024biological_processglycosaminoglycan biosynthetic process
A0006065biological_processUDP-glucuronate biosynthetic process
A0015012biological_processheparan sulfate proteoglycan biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0030206biological_processchondroitin sulfate biosynthetic process
A0034214biological_processprotein hexamerization
A0042802molecular_functionidentical protein binding
A0048666biological_processneuron development
A0051287molecular_functionNAD binding
A0070062cellular_componentextracellular exosome
B0001702biological_processgastrulation with mouth forming second
B0003979molecular_functionUDP-glucose 6-dehydrogenase activity
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0006024biological_processglycosaminoglycan biosynthetic process
B0006065biological_processUDP-glucuronate biosynthetic process
B0015012biological_processheparan sulfate proteoglycan biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0030206biological_processchondroitin sulfate biosynthetic process
B0034214biological_processprotein hexamerization
B0042802molecular_functionidentical protein binding
B0048666biological_processneuron development
B0051287molecular_functionNAD binding
B0070062cellular_componentextracellular exosome
C0001702biological_processgastrulation with mouth forming second
C0003979molecular_functionUDP-glucose 6-dehydrogenase activity
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005829cellular_componentcytosol
C0006024biological_processglycosaminoglycan biosynthetic process
C0006065biological_processUDP-glucuronate biosynthetic process
C0015012biological_processheparan sulfate proteoglycan biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0030206biological_processchondroitin sulfate biosynthetic process
C0034214biological_processprotein hexamerization
C0042802molecular_functionidentical protein binding
C0048666biological_processneuron development
C0051287molecular_functionNAD binding
C0070062cellular_componentextracellular exosome
D0001702biological_processgastrulation with mouth forming second
D0003979molecular_functionUDP-glucose 6-dehydrogenase activity
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005829cellular_componentcytosol
D0006024biological_processglycosaminoglycan biosynthetic process
D0006065biological_processUDP-glucuronate biosynthetic process
D0015012biological_processheparan sulfate proteoglycan biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0030206biological_processchondroitin sulfate biosynthetic process
D0034214biological_processprotein hexamerization
D0042802molecular_functionidentical protein binding
D0048666biological_processneuron development
D0051287molecular_functionNAD binding
D0070062cellular_componentextracellular exosome
E0001702biological_processgastrulation with mouth forming second
E0003979molecular_functionUDP-glucose 6-dehydrogenase activity
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005829cellular_componentcytosol
E0006024biological_processglycosaminoglycan biosynthetic process
E0006065biological_processUDP-glucuronate biosynthetic process
E0015012biological_processheparan sulfate proteoglycan biosynthetic process
E0016491molecular_functionoxidoreductase activity
E0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E0030206biological_processchondroitin sulfate biosynthetic process
E0034214biological_processprotein hexamerization
E0042802molecular_functionidentical protein binding
E0048666biological_processneuron development
E0051287molecular_functionNAD binding
E0070062cellular_componentextracellular exosome
F0001702biological_processgastrulation with mouth forming second
F0003979molecular_functionUDP-glucose 6-dehydrogenase activity
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005829cellular_componentcytosol
F0006024biological_processglycosaminoglycan biosynthetic process
F0006065biological_processUDP-glucuronate biosynthetic process
F0015012biological_processheparan sulfate proteoglycan biosynthetic process
F0016491molecular_functionoxidoreductase activity
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0030206biological_processchondroitin sulfate biosynthetic process
F0034214biological_processprotein hexamerization
F0042802molecular_functionidentical protein binding
F0048666biological_processneuron development
F0051287molecular_functionNAD binding
F0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG4 A 467
ChainResidue
APHE265
APHE272
AGLY273
APHE277
APHE338
ALYS339
AHOH678
AHOH761
AHOH805

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 468
ChainResidue
AGLN390
AARG393
CTYR96

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PG4 C 467
ChainResidue
CPHE265
CLYS267
CPHE272
CGLY273
CPHE277
CHOH477
CHOH1147

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PG4 C 468
ChainResidue
CMET358
CASP359
CGLN390
CARG393
ETYR96

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO C 469
ChainResidue
CHIS201
CHOH790

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 D 467
ChainResidue
DPHE265
DLYS267
DGLY273
DPHE277
DPHE338
DHOH1163

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 468
ChainResidue
BTYR96
DMET358
DGLN390
DHOH806
DHOH991

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 470
ChainResidue
DPHE162
DASP171
DASP176
DARG177

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 471
ChainResidue
DTYR96
FMET358
FGLN390
FARG393

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO E 468
ChainResidue
ATYR96
EGLN390

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 467
ChainResidue
BHOH721

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 468
ChainResidue
BGLU29
BARG31
BLYS67
BHOH538

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 469
ChainResidue
BASP171
BASP176

site_idBC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PG4 F 467
ChainResidue
FLEU163
FGLU165
FPHE272
FGLY273
FPHE277
FPHE338
FLYS339
FARG442
FHOH491
FHOH654
FHOH717
FHOH1093

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO F 468
ChainResidue
FGLY13
FTYR14
FARG346

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO F 469
ChainResidue
FARG41
FPRO51
FILE52

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO F 470
ChainResidue
FHIS201
FHOH863

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:22123821
ChainResidueDetails
AGLU161
ELYS220
FGLU161
FLYS220
ALYS220
BGLU161
BLYS220
CGLU161
CLYS220
DGLU161
DLYS220
EGLU161

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21984906, ECO:0000269|PubMed:22123821
ChainResidueDetails
ACYS276
BCYS276
CCYS276
DCYS276
ECYS276
FCYS276

site_idSWS_FT_FI3
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK
ChainResidueDetails
AGLY11
BCYS276
CGLY11
CASP36
CARG41
CVAL89
CCYS276
DGLY11
DASP36
DARG41
DVAL89
AASP36
DCYS276
EGLY11
EASP36
EARG41
EVAL89
ECYS276
FGLY11
FASP36
FARG41
FVAL89
AARG41
FCYS276
AVAL89
ACYS276
BGLY11
BASP36
BARG41
BVAL89

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445
ChainResidueDetails
ASER130
BSER130
CSER130
DSER130
ESER130
FSER130

site_idSWS_FT_FI5
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF
ChainResidueDetails
AGLU161
CLYS220
CLYS267
CPHE338
DGLU161
DLYS220
DLYS267
DPHE338
EGLU161
ELYS220
ELYS267
ALYS220
EPHE338
FGLU161
FLYS220
FLYS267
FPHE338
ALYS267
APHE338
BGLU161
BLYS220
BLYS267
BPHE338
CGLU161

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21502315, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4
ChainResidueDetails
AGLU165
BGLU165
CGLU165
DGLU165
EGLU165
FGLU165

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23106432, ECO:0000269|PubMed:27966912, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF, ECO:0007744|PDB:5TJH
ChainResidueDetails
AARG260
BARG260
CARG260
DARG260
EARG260
FARG260

site_idSWS_FT_FI8
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445, ECO:0000269|PubMed:21984906, ECO:0000269|PubMed:22123821, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:3TDK
ChainResidueDetails
AARG346
BARG346
CARG346
DARG346
EARG346
FARG346

site_idSWS_FT_FI9
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22123821, ECO:0000269|PubMed:23106432, ECO:0000305|PubMed:21502315, ECO:0000305|PubMed:21595445, ECO:0007744|PDB:2QG4, ECO:0007744|PDB:3KHU, ECO:0007744|PDB:3PRJ, ECO:0007744|PDB:3PTZ, ECO:0007744|PDB:4EDF
ChainResidueDetails
AARG442
BARG442
CARG442
DARG442
EARG442
FARG442

site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS107
BLYS107
CLYS107
DLYS107
ELYS107
FLYS107

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dli
ChainResidueDetails
AASP280
AASN224
ACYS276
ALYS220
ASER130
AGLU165

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dli
ChainResidueDetails
BASP280
BASN224
BCYS276
BLYS220
BSER130
BGLU165

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dli
ChainResidueDetails
CASP280
CASN224
CCYS276
CLYS220
CSER130
CGLU165

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dli
ChainResidueDetails
DASP280
DASN224
DCYS276
DLYS220
DSER130
DGLU165

site_idCSA5
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dli
ChainResidueDetails
EASP280
EASN224
ECYS276
ELYS220
ESER130
EGLU165

site_idCSA6
Number of Residues6
DetailsAnnotated By Reference To The Literature 1dli
ChainResidueDetails
FASP280
FASN224
FCYS276
FLYS220
FSER130
FGLU165

227561

PDB entries from 2024-11-20

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