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1PDY

X-RAY STRUCTURE AND CATALYTIC MECHANISM OF LOBSTER ENOLASE

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 440
ChainResidue
ALYS344
AARG373
ASER374
AHOH540
AHOH542

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKvNQIGSVTES
ChainResidueDetails
ALEU341-SER354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU209

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ALYS344

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AASP244
AGLU294
AASP319
ALYS344
ASER371
ASER374
ALYS395
ASER36
AHIS157
AGLU166

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:7547999
ChainResidueDetails
ASER1

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PDB entries from 2024-05-01

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