Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ZLF

Structure of group A Streptococcal enolase K312A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006096biological_processglycolytic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006096biological_processglycolytic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
C0000015cellular_componentphosphopyruvate hydratase complex
C0000287molecular_functionmagnesium ion binding
C0004634molecular_functionphosphopyruvate hydratase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005886cellular_componentplasma membrane
C0006096biological_processglycolytic process
C0009274cellular_componentpeptidoglycan-based cell wall
C0009986cellular_componentcell surface
C0016829molecular_functionlyase activity
C0046872molecular_functionmetal ion binding
D0000015cellular_componentphosphopyruvate hydratase complex
D0000287molecular_functionmagnesium ion binding
D0004634molecular_functionphosphopyruvate hydratase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005886cellular_componentplasma membrane
D0006096biological_processglycolytic process
D0009274cellular_componentpeptidoglycan-based cell wall
D0009986cellular_componentcell surface
D0016829molecular_functionlyase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 436
ChainResidue
AGLN163
AHOH2115
AGLU164
AGLU205
ALYS344
AHIS372
AARG373
ASER374
ALYS395
APO4437

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 437
ChainResidue
AGLY40
AALA41
ASER42
ALYS344
AARG373
ASER374
APO4436
AHOH2028
AHOH2029

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 436
ChainResidue
BARG16
BALA41
BSER374
BPO4437
BHOH2021

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 437
ChainResidue
BLYS344
BARG373
BSER374
BPO4436
BHOH2021

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 C 436
ChainResidue
CGLN163
CGLU164
CGLU205
CLYS344
CHIS372
CARG373
CSER374
CLYS395
CPO4437

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 C 437
ChainResidue
CGLY40
CALA41
CSER42
CLYS344
CARG373
CSER374
CPO4436

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 D 436
ChainResidue
DGLN163
DGLU164
DGLU205
DASP243
DLYS344
DHIS372
DSER374
DLYS395
DPO4437

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 D 437
ChainResidue
DGLY40
DALA41
DSER42
DLYS344
DARG373
DSER374
DPO4436
DHOH2028

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKvNQIGTLTET
ChainResidueDetails
AILE341-THR354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsSite: {"description":"Important for binding of plasminogen","evidences":[{"source":"PubMed","id":"14688086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon