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2AKZ

Fluoride Inhibition of Enolase: Crystal Structure of the Inhibitory Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0001917cellular_componentphotoreceptor inner segment
A0004634molecular_functionphosphopyruvate hydratase activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0043025cellular_componentneuronal cell body
A0043204cellular_componentperikaryon
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0001917cellular_componentphotoreceptor inner segment
B0004634molecular_functionphosphopyruvate hydratase activity
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0043025cellular_componentneuronal cell body
B0043204cellular_componentperikaryon
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG A 440
ChainResidue
AASP244
AGLU292
AASP317
ALYS342
AMG441
AF444
AF445
AHOH461

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 441
ChainResidue
AMG440
APO4442
AF444
AHOH462
AHOH463
ASER39

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MG B 1440
ChainResidue
BASP1244
BGLU1292
BASP1317
BLYS1342
BMG1441
BF1444
BF1445
BHOH1446

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 1441
ChainResidue
BSER1039
BASP1317
BMG1440
BPO41442
BF1444
BHOH1447
BHOH1448

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 A 442
ChainResidue
AGLY37
AALA38
ASER39
AHIS157
AGLN165
ALYS342
AARG371
ASER372
AMG441
AF444
AF445
AHOH463
AHOH527

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 B 1442
ChainResidue
BHOH151
BGLY1037
BALA1038
BSER1039
BHIS1157
BGLN1165
BLYS1342
BARG1371
BSER1372
BMG1441
BF1444
BF1445
BHOH1448

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE F A 444
ChainResidue
ASER39
AGLN165
AASP244
AASP317
AMG440
AMG441
APO4442
AF445
AHOH461
AHOH462
AHOH463

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F A 445
ChainResidue
AGLU166
AASP244
AGLU292
AASP317
ALEU340
ALYS342
ALYS393
AMG440
APO4442
AF444

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE F B 1444
ChainResidue
BSER1039
BGLN1165
BASP1244
BASP1317
BMG1440
BMG1441
BPO41442
BF1445
BHOH1446
BHOH1447
BHOH1448

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F B 1445
ChainResidue
BGLU1166
BASP1244
BGLU1292
BASP1317
BLEU1340
BLYS1342
BLYS1393
BMG1440
BPO41442
BF1444

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS A 460
ChainResidue
ASER248
AGLU249
AGLN297
AHOH519
AHOH557
AHOH577
AHOH589
AHOH945
ATHR40
AILE42

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKvNQIGSVTEA
ChainResidueDetails
ALEU339-ALA352

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
AGLY210
BGLY1210

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
AVAL343
BVAL1343

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ATHR40
BTHR1040

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
AALA158
BASP1318
BHIS1370
BTHR1394
APHE167
AASP293
AASP318
AHIS370
ATHR394
BALA1158
BPHE1167
BASP1293

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AVAL245
BVAL1245

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
AILE2
BILE1002

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
AILE5
AALA64
AGLY193
ATYR256
BILE1005
BALA1064
BGLY1193
BTYR1256

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
AALA26
BALA1026

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
AGLU44
BGLU1044

site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
AGLY60
ALEU89
AGLU228
BGLY1060
BLEU1089
BGLU1228

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17183
ChainResidueDetails
AASP197
ATYR199
BASP1197
BTYR1199

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
AASP202
BASP1202

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
AALA233
BALA1233

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO263
BPRO1263

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
APRO287
BPRO1287

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
AILE291
BILE1291

site_idSWS_FT_FI17
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
AALA335
AVAL343
ATYR406
BALA1335
BVAL1343
BTYR1406

site_idSWS_FT_FI18
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
AASP202
BASP1202

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AGLU209
AGLU166
AHIS370
ALYS393

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BGLU1209
BGLU1166
BHIS1370
BLYS1393

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
ALYS342
AGLU209
AGLU166
AHIS370

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BGLU1209
BGLU1166
BLYS1342
BHIS1370

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
ALYS342
AHIS189

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BHIS1189
BLYS1342

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
ALYS342
AVAL240

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BLYS1342
BVAL1240

224004

PDB entries from 2024-08-21

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