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3UJ2

CRYSTAL STRUCTURE OF AN ENOLASE FROM ANAEROSTIPES CACCAE (EFI TARGET EFI-502054) WITH BOUND MG AND SULFATE

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
E0000015cellular_componentphosphopyruvate hydratase complex
E0000287molecular_functionmagnesium ion binding
E0004634molecular_functionphosphopyruvate hydratase activity
E0005576cellular_componentextracellular region
E0005737cellular_componentcytoplasm
E0006096biological_processglycolytic process
E0009986cellular_componentcell surface
E0016829molecular_functionlyase activity
E0046872molecular_functionmetal ion binding
F0000015cellular_componentphosphopyruvate hydratase complex
F0000287molecular_functionmagnesium ion binding
F0004634molecular_functionphosphopyruvate hydratase activity
F0005576cellular_componentextracellular region
F0005737cellular_componentcytoplasm
F0006096biological_processglycolytic process
F0009986cellular_componentcell surface
F0016829molecular_functionlyase activity
F0046872molecular_functionmetal ion binding
G0000015cellular_componentphosphopyruvate hydratase complex
G0000287molecular_functionmagnesium ion binding
G0004634molecular_functionphosphopyruvate hydratase activity
G0005576cellular_componentextracellular region
G0005737cellular_componentcytoplasm
G0006096biological_processglycolytic process
G0009986cellular_componentcell surface
G0016829molecular_functionlyase activity
G0046872molecular_functionmetal ion binding
H0000015cellular_componentphosphopyruvate hydratase complex
H0000287molecular_functionmagnesium ion binding
H0004634molecular_functionphosphopyruvate hydratase activity
H0005576cellular_componentextracellular region
H0005737cellular_componentcytoplasm
H0006096biological_processglycolytic process
H0009986cellular_componentcell surface
H0016829molecular_functionlyase activity
H0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 428
ChainResidue
AGLY42
AARG370
ASER371
AHOH533

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 429
ChainResidue
AARG178
AGLU179
AARG182
BARG60

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 430
ChainResidue
AASN20
ALYS64
AHOH790
AHOH1368
BHIS189
AARG18

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 431
ChainResidue
AASP244
AGLU289
AASP316
AHOH442
AHOH470
AHOH1536

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 428
ChainResidue
AARG60
BGLU179
BARG182

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 429
ChainResidue
BGLY42
BARG370
BSER371
BHOH745

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 430
ChainResidue
AHOH684
BARG18
BASN20
BLYS64
BHOH479

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 431
ChainResidue
BASP244
BGLU289
BASP316
BHOH962
BHOH1542
BHOH1543

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 428
ChainResidue
CGLY42
CARG370
CSER371
CHOH1570

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 429
ChainResidue
CARG178
CGLU179
CARG182
DARG60

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 430
ChainResidue
CGLU218
CARG265
CARG265
CHIS275
CSER278
CARG282

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 431
ChainResidue
CASP244
CGLU289
CASP316
CHOH482
CHOH958
CHOH968

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 428
ChainResidue
CARG60
DARG178
DGLU179
DARG182

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 429
ChainResidue
DGLY42
DARG370
DSER371

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 430
ChainResidue
DASP244
DGLU289
DASP316
DHOH431
DHOH453
DHOH1584

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 428
ChainResidue
EGLY42
ELYS341
EARG370
ESER371

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 429
ChainResidue
EARG178
EGLU179
EARG182
FARG60

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG E 430
ChainResidue
EGLN165
EASP244
EGLU289
EASP316
EHOH443
EHOH1233
EHOH1612

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 F 428
ChainResidue
EARG60
FARG178
FGLU179
FARG182

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 F 429
ChainResidue
FGLY42
FARG370
FSER371

site_idCC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG F 430
ChainResidue
FASP244
FGLU289
FASP316
FHOH432
FHOH961
FHOH1621

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 G 428
ChainResidue
GARG178
GGLU179
GARG182
HARG60

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 G 429
ChainResidue
GARG18
GASN20
GLYS64
GHOH521
HHIS189

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 G 430
ChainResidue
GGLY42
GARG370
GSER371

site_idCC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG G 431
ChainResidue
GASP244
GGLU289
GASP316
GHOH439
GHOH1220
GHOH1228

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 H 428
ChainResidue
HGLY42
HARG370
HSER371
HHOH1264

site_idCC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 H 429
ChainResidue
GARG60
HGLU179
HARG182

site_idDC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG H 430
ChainResidue
HGLN165
HASP244
HGLU289
HASP316
HHOH980
HHOH1649

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKlNQIGTVSET
ChainResidueDetails
AILE338-THR351

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PDB entries from 2025-07-30

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