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3QN3

Phosphopyruvate hydratase from Campylobacter jejuni.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
C0000015cellular_componentphosphopyruvate hydratase complex
C0000287molecular_functionmagnesium ion binding
C0004634molecular_functionphosphopyruvate hydratase activity
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0006096biological_processglycolytic process
C0009986cellular_componentcell surface
C0016829molecular_functionlyase activity
C0046872molecular_functionmetal ion binding
D0000015cellular_componentphosphopyruvate hydratase complex
D0000287molecular_functionmagnesium ion binding
D0004634molecular_functionphosphopyruvate hydratase activity
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0006096biological_processglycolytic process
D0009986cellular_componentcell surface
D0016829molecular_functionlyase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AASP239
AGLU280
AASP307
AHOH467
AHOH545
AHOH572

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BHOH416
BHOH452
BHOH567
BASP239
BGLU280
BASP307

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 601
ChainResidue
CASP239
CGLU280
CASP307
CHOH446
CHOH544
CHOH568

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 601
ChainResidue
DASP239
DGLU280
DASP307
DHOH439
DHOH459
DHOH475

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD C 415
ChainResidue
CLYS22
CALA35
CARG119
CASP367

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD D 602
ChainResidue
DLYS22
DARG119
DGLU366
DASP367

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD B 603
ChainResidue
AGOL605
BLYS22
BALA34
BGLU366
BASP367
BHOH422

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 604
ChainResidue
ALYS22
AALA34
AASP367
AHOH427

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 605
ChainResidue
AALA368
AALA394
AGLU401
BLYS22
BILE36
BGLU366
BMPD603

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 606
ChainResidue
CSER195
CHIS197

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 607
ChainResidue
CALA394
CASN397
CARG398
CGLU401
CHOH471
DLYS22
DILE36
DGLU366

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 608
ChainResidue
DGLY299
DLYS301
DILE302
DGLN303
DASN327

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 609
ChainResidue
BGLY299
BASN300
BLYS301
BILE302
BGLN303
BASN327

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 610
ChainResidue
CGLY299
CASN300
CILE302
CGLN303

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. VLIKpNQIGTITQT
ChainResidueDetails
AVAL329-THR342

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLU204
BGLU204
CGLU204
DGLU204

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS332
BLYS332
CLYS332
DLYS332

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLN162
BLYS383
CGLN162
CLYS332
CARG361
CSER362
CLYS383
DGLN162
DLYS332
DARG361
DSER362
ALYS332
DLYS383
AARG361
ASER362
ALYS383
BGLN162
BLYS332
BARG361
BSER362

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0007744|PDB:3QN3
ChainResidueDetails
AASP239
DASP239
DGLU280
DASP307
AGLU280
AASP307
BASP239
BGLU280
BASP307
CASP239
CGLU280
CASP307

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PDB entries from 2024-07-24

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