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1U0E

Crystal structure of mouse phosphoglucose isomerase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001701biological_processin utero embryonic development
A0001707biological_processmesoderm formation
A0002639biological_processpositive regulation of immunoglobulin production
A0004347molecular_functionglucose-6-phosphate isomerase activity
A0005125molecular_functioncytokine activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006002biological_processfructose 6-phosphate metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0007165biological_processsignal transduction
A0007611biological_processlearning or memory
A0008083molecular_functiongrowth factor activity
A0010595biological_processpositive regulation of endothelial cell migration
A0016853molecular_functionisomerase activity
A0031625molecular_functionubiquitin protein ligase binding
A0032355biological_processresponse to estradiol
A0032570biological_processresponse to progesterone
A0033574biological_processresponse to testosterone
A0034101biological_processerythrocyte homeostasis
A0035902biological_processresponse to immobilization stress
A0035994biological_processresponse to muscle stretch
A0042593biological_processglucose homeostasis
A0043209cellular_componentmyelin sheath
A0043524biological_processnegative regulation of neuron apoptotic process
A0046686biological_processresponse to cadmium ion
A0048029molecular_functionmonosaccharide binding
A0051156biological_processglucose 6-phosphate metabolic process
A0060170cellular_componentciliary membrane
A0061620biological_processglycolytic process through glucose-6-phosphate
A0061621biological_processcanonical glycolysis
A0097367molecular_functioncarbohydrate derivative binding
A1901135biological_processcarbohydrate derivative metabolic process
B0001701biological_processin utero embryonic development
B0001707biological_processmesoderm formation
B0002639biological_processpositive regulation of immunoglobulin production
B0004347molecular_functionglucose-6-phosphate isomerase activity
B0005125molecular_functioncytokine activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006002biological_processfructose 6-phosphate metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0007165biological_processsignal transduction
B0007611biological_processlearning or memory
B0008083molecular_functiongrowth factor activity
B0010595biological_processpositive regulation of endothelial cell migration
B0016853molecular_functionisomerase activity
B0031625molecular_functionubiquitin protein ligase binding
B0032355biological_processresponse to estradiol
B0032570biological_processresponse to progesterone
B0033574biological_processresponse to testosterone
B0034101biological_processerythrocyte homeostasis
B0035902biological_processresponse to immobilization stress
B0035994biological_processresponse to muscle stretch
B0042593biological_processglucose homeostasis
B0043209cellular_componentmyelin sheath
B0043524biological_processnegative regulation of neuron apoptotic process
B0046686biological_processresponse to cadmium ion
B0048029molecular_functionmonosaccharide binding
B0051156biological_processglucose 6-phosphate metabolic process
B0060170cellular_componentciliary membrane
B0061620biological_processglycolytic process through glucose-6-phosphate
B0061621biological_processcanonical glycolysis
B0097367molecular_functioncarbohydrate derivative binding
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1201
ChainResidue
ASER159
ASER209
ALYS210
ATHR211
ATHR214
AHOH1259
AHOH1479
AHOH1638
AHOH1739

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1202
ChainResidue
AALA1
AALA2
AARG5
ASER366
AALA368
AHOH1364
AHOH1442

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1203
ChainResidue
BARG136
BHOH1279
BHOH1513
BHOH1612

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1204
ChainResidue
BALA368
BARG369
BHOH1613

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1205
ChainResidue
BGLY158
BGLY271
BARG272
BGLN353
BHOH1366
BHOH1544
BHOH1704

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1206
ChainResidue
AASN46
AHIS47
AHOH1527
AHOH1745

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1207
ChainResidue
AARG105
ASER297
AHOH1526

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1208
ChainResidue
BLYS146
BSER147
BHOH1283
BHOH1375

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1209
ChainResidue
BTHR211
BTHR213
BTHR214
BHOH1448
BHOH1490
BHOH1645

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 1210
ChainResidue
ALYS522
AHOH1595
BGLY530
BSER531
BSER532
BHOH1552
BHOH1624
BHOH1641

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 1211
ChainResidue
AGLY418
AHOH1353
AHOH1438
BARG552

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME A 1212
ChainResidue
AARG346
AGOL1225
AHOH1640
BGLN342
BHOH1352
BHOH1511

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A 1213
ChainResidue
AHIS49
BGLN551

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 1214
ChainResidue
ATHR149
AARG179
AHOH1545
AHOH1716

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 1215
ChainResidue
ALEU195
ALEU198
ATRP227
AHOH1451

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1221
ChainResidue
AARG134
AASP139
ATRP140
ALYS141
ALYS240
AHOH1569
AHOH1616
AHOH1625

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1222
ChainResidue
BGLN8
BSER73
BHOH1505
BHOH1534
BHOH1536

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 1223
ChainResidue
AASN470
AARG471

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1224
ChainResidue
BASN38
BTYR54
BLYS61
BMET64
BHOH1321
BHOH1498

site_idCC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1225
ChainResidue
ABME1212
AHOH1446
AHOH1536
AHOH1639
AGLU168
APHE182
AHIS345

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1226
ChainResidue
APHE131
AVAL243
AGLN260
AASN261
ALEU263
AHOH1443
AHOH1624

site_idCC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1227
ChainResidue
ALYS171
AARG179
AVAL180
AHIS286
AHOH1400
AHOH1529
AHOH1581
AHOH1608
AHOH1637

Functional Information from PROSITE/UniProt
site_idPS00174
Number of Residues18
DetailsP_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiMWdinsFDQwGVElgK
ChainResidueDetails
AGLY501-LYS518

site_idPS00765
Number of Residues14
DetailsP_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG
ChainResidueDetails
AASP267-GLY280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:15342241
ChainResidueDetails
ASER358
BSER358

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:15342241
ChainResidueDetails
AALA389
AGLN519
BALA389
BGLN519

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15342241, ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F, ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT
ChainResidueDetails
ASER159
BSER358
BALA389
BGLN519
ALYS210
AGLY354
ASER358
AALA389
AGLN519
BSER159
BLYS210
BGLY354

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
ALEU12
BLEU12

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6P6V0
ChainResidueDetails
AGLY86
BGLY86

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
AASN107
BASN107

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
APRO109
BPRO109

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
AGLY142
BGLY142

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744
ChainResidueDetails
AASN185
BASN185

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0
ChainResidueDetails
AALA250
BALA250

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ASER454
BSER454

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
APRO455
BPRO455

218853

PDB entries from 2024-04-24

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