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2XSX

Crystal structure of human beta enolase ENOB

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 500
ChainResidue
AASP245
AGLU293
AASP318
AHOH2267
AHOH2358
AHOH2506

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
ASER373
AHOH2506
AHOH2542
AHOH2543
AGLU210
ALYS343
AARG372

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
ALYS193
ATHR205
AVAL207
AHOH2544
BASP209

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
ALYS202
AASP203
AALA204
ATHR205
AASN206
BGLY160
BHOH2301

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
AGLU219
AASN220
AASN221
AHOH2545

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 505
ChainResidue
AGLY273
AGLU274
AGLY277
APHE296
ATHR303
ASER306
APHE307
AHOH2396
AHOH2546

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AGLU180
AARG183
AILE184
ATYR236
AHOH2547

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 507
ChainResidue
ALYS202
AGLY310
AVAL311
AASN312
AEDO508
AHOH2548
BPHE261
BLYS262

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 508
ChainResidue
ALYS202
AVAL311
AASN312
AEDO507
AHOH2549
AHOH2550
BLYS262
BSER263
BPRO264

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 509
ChainResidue
AALA302
AHOH2288
AHOH2553
AHOH2554
AHOH2555
BLEU58

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 510
ChainResidue
AASN338
AHOH2462
AHOH2556
AHOH2557

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 511
ChainResidue
AGLU21
AARG32
AASP378
AHOH2558

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 500
ChainResidue
BASP245
BGLU293
BASP318
BHOH2254
BHOH2336
BHOH2514

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
BGLU210
BLYS343
BARG372
BSER373
BHOH2514

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 502
ChainResidue
AGLY160
AHOH2318
BLYS202
BASP203
BALA204
BTHR205
BASN206

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 503
ChainResidue
BGLU219
BASN220
BASN221
BHOH2515

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 504
ChainResidue
BEDO510
BHOH2516
BHOH2517
BHOH2518
BHIS191
BGLY194
BVAL195

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 505
ChainResidue
AGLU10
AHOH2015
AHOH2017
BLYS179
BGLU415
BHOH2264

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 506
ChainResidue
AASP209
BLYS193
BTHR205
BASN206
BHOH2519

site_idCC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 507
ChainResidue
BASP142
BLEU143
BILE144
BILE422
BHOH2492
BHOH2520
BHOH2521

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 508
ChainResidue
BGLU274
BPHE307
BHOH2522

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 509
ChainResidue
BGLU180
BARG183
BTYR236
BHOH2334
BHOH2523

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 510
ChainResidue
ALEU58
BGLY194
BEDO504

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKvNQIGSVTES
ChainResidueDetails
ALEU340-SER353

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU210
BGLU210

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ALYS343
BLYS343

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS158
BASP245
BGLU293
BASP318
BSER370
BLYS394
AGLU167
AASP245
AGLU293
AASP318
ASER370
ALYS394
BHIS158
BGLU167

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P15429
ChainResidueDetails
ATHR72
ATHR205
ATHR229
BTHR72
BTHR205
BTHR229

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P15429
ChainResidueDetails
ASER83
ASER157
BSER83
BSER157

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER176
ASER263
BSER176
BSER263

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P15429
ChainResidueDetails
ATYR236
BTYR236

218853

PDB entries from 2024-04-24

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