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1T2A

Crystal structure of human GDP-D-mannose 4,6-dehydratase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007219biological_processNotch signaling pathway
A0008446molecular_functionGDP-mannose 4,6-dehydratase activity
A0016829molecular_functionlyase activity
A0019673biological_processGDP-mannose metabolic process
A0042350biological_processGDP-L-fucose biosynthetic process
A0042351biological_process'de novo' GDP-L-fucose biosynthetic process
A0042802molecular_functionidentical protein binding
A0070062cellular_componentextracellular exosome
A0070401molecular_functionNADP+ binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0007219biological_processNotch signaling pathway
B0008446molecular_functionGDP-mannose 4,6-dehydratase activity
B0016829molecular_functionlyase activity
B0019673biological_processGDP-mannose metabolic process
B0042350biological_processGDP-L-fucose biosynthetic process
B0042351biological_process'de novo' GDP-L-fucose biosynthetic process
B0042802molecular_functionidentical protein binding
B0070062cellular_componentextracellular exosome
B0070401molecular_functionNADP+ binding
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0007219biological_processNotch signaling pathway
C0008446molecular_functionGDP-mannose 4,6-dehydratase activity
C0016829molecular_functionlyase activity
C0019673biological_processGDP-mannose metabolic process
C0042350biological_processGDP-L-fucose biosynthetic process
C0042351biological_process'de novo' GDP-L-fucose biosynthetic process
C0042802molecular_functionidentical protein binding
C0070062cellular_componentextracellular exosome
C0070401molecular_functionNADP+ binding
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0007219biological_processNotch signaling pathway
D0008446molecular_functionGDP-mannose 4,6-dehydratase activity
D0016829molecular_functionlyase activity
D0019673biological_processGDP-mannose metabolic process
D0042350biological_processGDP-L-fucose biosynthetic process
D0042351biological_process'de novo' GDP-L-fucose biosynthetic process
D0042802molecular_functionidentical protein binding
D0070062cellular_componentextracellular exosome
D0070401molecular_functionNADP+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues39
DetailsBINDING SITE FOR RESIDUE NDP A 1001
ChainResidue
AGLY30
AGLY109
AALA110
ASER112
ATYR123
AVAL127
AALA153
ASER154
ATHR155
ATYR179
ALYS183
ATHR32
ALEU206
AASN208
AHIS209
AARG214
AHOH1004
AHOH1010
AHOH1013
AHOH1015
AHOH1017
AHOH1021
AGLY33
AHOH1031
AHOH1039
AHOH1059
AHOH1071
AHOH1147
AHOH1190
DARG56
DSER57
DSER58
DHOH1320
AGLN34
AASP35
AARG55
AASP86
ALEU87
ALEU108

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP A 1002
ChainResidue
AVAL114
AASN208
AASN217
APHE218
AVAL219
ALYS222
ALEU240
AGLY241
AASN242
AALA245
AARG247
AVAL281
ATYR323
AARG325
AGLU328
AHOH1011
AHOH1036
AHOH1042
AHOH1045
AHOH1046
AHOH1064
AHOH1174

site_idAC3
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NDP B 1101
ChainResidue
BGLY30
BTHR32
BGLY33
BGLN34
BASP35
BARG55
BASP86
BLEU87
BLEU108
BGLY109
BALA110
BSER112
BTYR123
BVAL127
BALA153
BSER154
BTHR155
BTYR179
BLYS183
BLEU206
BASN208
BHIS209
BARG214
BHOH1111
BHOH1113
BHOH1119
BHOH1128
BHOH1131
BHOH1132
BHOH1152
BHOH1196
BHOH1256
BHOH1271
BHOH1341
CARG56
CSER58
CHOH1244

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GDP B 1102
ChainResidue
BGLU157
BASN208
BASN217
BVAL219
BLYS222
BLEU240
BGLY241
BASN242
BALA245
BARG247
BVAL281
BARG325
BGLU328
BHOH1109
BHOH1122
BHOH1129
BHOH1133
BHOH1223
BHOH1274
BHIS113

site_idAC5
Number of Residues39
DetailsBINDING SITE FOR RESIDUE NDP C 1201
ChainResidue
BARG56
BSER57
BSER58
CGLY30
CTHR32
CGLY33
CGLN34
CASP35
CARG55
CASP86
CLEU87
CLEU108
CGLY109
CALA110
CSER112
CTYR123
CVAL127
CALA153
CSER154
CTHR155
CTYR179
CLYS183
CLEU206
CASN208
CHIS209
CARG214
CHOH1205
CHOH1206
CHOH1210
CHOH1211
CHOH1213
CHOH1217
CHOH1227
CHOH1230
CHOH1235
CHOH1316
CHOH1341
CHOH1344
CHOH1345

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDP C 1202
ChainResidue
CVAL114
CGLU157
CASN208
CASN217
CVAL219
CLYS222
CLEU240
CGLY241
CASN242
CALA245
CARG247
CVAL281
CTYR323
CARG325
CGLU328
CHOH1226
CHOH1232
CHOH1236
CHOH1241
CHOH1250
CHOH1300
CHOH1334

site_idAC7
Number of Residues39
DetailsBINDING SITE FOR RESIDUE NDP D 1301
ChainResidue
AARG56
ASER57
ASER58
AHOH1205
DGLY30
DTHR32
DGLY33
DGLN34
DASP35
DARG55
DASP86
DLEU87
DLEU108
DGLY109
DALA110
DSER112
DTYR123
DVAL127
DALA153
DSER154
DTHR155
DTYR179
DLYS183
DLEU206
DASN208
DHIS209
DARG214
DHOH1303
DHOH1304
DHOH1307
DHOH1316
DHOH1321
DHOH1330
DHOH1343
DHOH1344
DHOH1345
DHOH1367
DHOH1461
DHOH1483

site_idAC8
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP D 1302
ChainResidue
DHIS113
DVAL114
DGLU157
DASN208
DASN217
DPHE218
DVAL219
DLYS222
DLEU240
DGLY241
DASN242
DALA245
DARG247
DVAL281
DTYR323
DARG325
DGLU328
DHOH1312
DHOH1317
DHOH1318
DHOH1327
DHOH1348
DHOH1376
DHOH1425

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. PqkettpfypRspYGAAKLYAyWIVvNFR
ChainResidueDetails
APRO166-ARG194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ATHR155
BTHR155
CTHR155
DTHR155

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AGLU157
ATYR179
BGLU157
BTYR179
CGLU157
CTYR179
DGLU157
DTYR179

site_idSWS_FT_FI3
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|Ref.9
ChainResidueDetails
AGLY30
BARG55
BASP86
BLEU108
BTYR123
BLYS183
BHIS209
BARG214
CGLY30
CARG55
CASP86
AARG55
CLEU108
CTYR123
CLYS183
CHIS209
CARG214
DGLY30
DARG55
DASP86
DLEU108
DTYR123
AASP86
DLYS183
DHIS209
DARG214
ALEU108
ATYR123
ALYS183
AHIS209
AARG214
BGLY30

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR323
BTYR323
CTYR323
DTYR323

220113

PDB entries from 2024-05-22

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