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2B69

Crystal Structure of Human UDP-glucoronic acid decarboxylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0042732biological_processD-xylose metabolic process
A0048040molecular_functionUDP-glucuronate decarboxylase activity
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE NAD A 800
ChainResidue
AGLY11
ATHR39
AGLY40
AHIS59
AASP60
AVAL61
ALEU75
AALA76
ASER77
AALA79
ATHR94
AALA13
ASER117
ATHR118
ATYR147
ALYS151
AILE174
AASN176
ATHR177
AARG188
AHOH905
AHOH922
AGLY14
AHOH925
AHOH969
AHOH999
APHE15
AVAL16
AASP35
AASN36
APHE37
APHE38

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE UDP A 900
ChainResidue
APRO81
AARG144
AASN176
AARG188
AVAL189
AASN192
ATHR204
AVAL205
ATYR206
AGLN211
AARG213
AILE247
AASP273
AARG277
AHOH934
AHOH940
AHOH942
AHOH980
AHOH1029

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UDP A 901
ChainResidue
APRO64
ALEU65
ATYR66
ALEU100
AASN101
AGLY104
ALEU105
ALYS107
AARG108
ATYR161
AHOH918
AHOH929
AHOH981
AHOH985
AHOH1183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:23656592, ECO:0000269|PubMed:25521717
ChainResidueDetails
ATYR147

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:22810237, ECO:0000269|PubMed:25521717, ECO:0007744|PDB:2B69, ECO:0007744|PDB:4LK3, ECO:0007744|PDB:4M55
ChainResidueDetails
AGLY14
AVAL61
ALEU75
ATHR94
ALYS151
ATHR177
AARG188
APHE15
AVAL16
AASP35
AASN36
APHE38
ATHR39
AGLY40
AASP60

site_idSWS_FT_FI3
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:25521717, ECO:0007744|PDB:4LK3
ChainResidueDetails
ALEU65
AGLN164
AGLU165
ATYR66
ALYS93
AASN101
AGLY104
ALYS107
AARG108
AALA116
ATYR161

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25521717, ECO:0007744|PDB:4M55
ChainResidueDetails
ASER77

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22810237, ECO:0007744|PDB:2B69
ChainResidueDetails
ATYR147

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:25521717, ECO:0007744|PDB:4LK3, ECO:0007744|PDB:4M55
ChainResidueDetails
AHIS183

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR10

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN232

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATHR118
ALYS151
ATYR147

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATHR118
AGLU120
ALYS151
ATYR147

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PDB entries from 2024-07-24

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