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1PDZ

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 Residues9
DetailsBINDING SITE FOR RESIDUE PGA A 439
ChainResidue
ASER36
AHIS157
AGLU209
ALYS344
AARG373
ASER374
AHOH441
AHOH444
AHOH569

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 440
ChainResidue
AASP244
AGLU294
AASP319
AHOH441
AHOH442
AHOH443

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 Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:7547999, ECO:0007744|PDB:1PDZ
ChainResidueDetails
ASER36
AHIS157
ALYS344
AARG373
ASER374

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:7547999, ECO:0007744|PDB:1PDZ
ChainResidueDetails
AASP244
AGLU294
AASP319

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000305|PubMed:7547999
ChainResidueDetails
ASER1

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
ALYS395
AHIS372
AGLU209
AGLU166

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AHIS372
AGLU209
AGLU166
ALYS344

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AHIS189
ALYS344

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PDB entries from 2024-11-06

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