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5WRO

Crystal structure of Drosophila enolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0006096biological_processglycolytic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CD A 601
ChainResidue
AGLY62
AHIS125
AHIS258
AHOH722
AHOH956

site_idAC2
Number of Residues6
Detailsbinding site for residue CD A 602
ChainResidue
AHOH707
AHOH720
AASP312
AGLU361
AASP386
ACL604

site_idAC3
Number of Residues3
Detailsbinding site for residue CO A 603
ChainResidue
AHIS225
AGLU277
AHOH725

site_idAC4
Number of Residues6
Detailsbinding site for residue CL A 604
ChainResidue
AASP386
ALYS411
ALYS462
ACD602
ASO4606
AHOH848

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 605
ChainResidue
ASER286
AASN287
ALYS288
ALEU347
APHE351
AHOH756

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 A 606
ChainResidue
AGLY105
AALA106
AARG440
ASER441
ACL604
AHOH848

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 607
ChainResidue
AARG99
ATYR198
AGLN477
AGLU484
AHOH713
AHOH858

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 608
ChainResidue
AARG82
AASN84
ALYS127
AHIS257
ALYS260
AHOH702

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKvNQIGTVTES
ChainResidueDetails
ALEU408-SER421

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU277

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ALYS411

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS225
AGLU234
AASP312
AGLU361
AASP386
ASER438
ALYS462

224201

PDB entries from 2024-08-28

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