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3OTR

2.75 Angstrom Crystal Structure of Enolase 1 from Toxoplasma gondii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
C0000015cellular_componentphosphopyruvate hydratase complex
C0000287molecular_functionmagnesium ion binding
C0004634molecular_functionphosphopyruvate hydratase activity
C0005737cellular_componentcytoplasm
C0006096biological_processglycolytic process
C0016829molecular_functionlyase activity
C0046872molecular_functionmetal ion binding
D0000015cellular_componentphosphopyruvate hydratase complex
D0000287molecular_functionmagnesium ion binding
D0004634molecular_functionphosphopyruvate hydratase activity
D0005737cellular_componentcytoplasm
D0006096biological_processglycolytic process
D0016829molecular_functionlyase activity
D0046872molecular_functionmetal ion binding
E0000015cellular_componentphosphopyruvate hydratase complex
E0000287molecular_functionmagnesium ion binding
E0004634molecular_functionphosphopyruvate hydratase activity
E0005737cellular_componentcytoplasm
E0006096biological_processglycolytic process
E0016829molecular_functionlyase activity
E0046872molecular_functionmetal ion binding
F0000015cellular_componentphosphopyruvate hydratase complex
F0000287molecular_functionmagnesium ion binding
F0004634molecular_functionphosphopyruvate hydratase activity
F0005737cellular_componentcytoplasm
F0006096biological_processglycolytic process
F0016829molecular_functionlyase activity
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL E 453
ChainResidue
EARG384
ESER385

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 F 453
ChainResidue
BLYS56
FLYS295
FLYS296
FTYR297
FPRO298

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKvNQIGSVTEA
ChainResidueDetails
ALEU352-ALA365

227111

PDB entries from 2024-11-06

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