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4RJT

Crystal Structure of Unliganded, Full Length hUGDH at pH 7.0

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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
AILE75
AASP76
AARG115

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
BILE75
BASP76
BARG115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:22123821
ChainResidueDetails
AGLU161
ALYS220
BGLU161
BLYS220
CGLU161
CLYS220

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21984906, ECO:0000269|PubMed:22123821
ChainResidueDetails
ACYS276
BCYS276
CCYS276

site_idSWS_FT_FI3
Number of Residues15
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
BASP36
BARG41
BVAL89
BCYS276
CGLY11
CASP36
CARG41
CVAL89
CCYS276
AGLY11
AVAL89
ACYS276
BGLY11
AASP36
AARG41

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21502315, ECO:0000269|PubMed:21595445
ChainResidueDetails
ASER130
BSER130
CSER130

site_idSWS_FT_FI5
Number of Residues12
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
BLYS267
BPHE338
CGLU161
CLYS220
CLYS267
CPHE338
AGLU161
ALYS220
ALYS267
APHE338
BGLU161
BLYS220

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21502315, ECO:0007744|PDB:2Q3E, ECO:0007744|PDB:2QG4
ChainResidueDetails
AGLU165
BGLU165
CGLU165

site_idSWS_FT_FI7
Number of Residues3
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

site_idSWS_FT_FI8
Number of Residues3
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

site_idSWS_FT_FI9
Number of Residues3
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

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS107
BLYS107
CLYS107

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER476
BSER476
CSER476

219869

PDB entries from 2024-05-15

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