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1YNS

Crystal Structure Of Human Enolase-phosphatase E1 and its complex with a substrate analog

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009086biological_processmethionine biosynthetic process
A0016787molecular_functionhydrolase activity
A0019509biological_processL-methionine salvage from methylthioadenosine
A0043874molecular_functionacireductone synthase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1258
ChainResidue
AASP16
AGLU18
AASP212
AHOH1831
AHOH1834
AHOH1835

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1259
ChainResidue
AHOH1837
AHOH1838
AHOH1839
AASP198
AHOH1832
AHOH1836

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1260
ChainResidue
AHOH1833
AHOH1840
AHOH1841
AHOH1842
AHOH1843
AHOH1844

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HPO A 1261
ChainResidue
AGLU18
ALEU31
APHE32
ATRP118
ASER153
ASER154
ALYS187
AHOH1313
AHOH1347
AHOH1463
AHOH1471
AHOH1477
AHOH1491
AHOH1598
AHOH1831

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03117","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15843022","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

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PDB entries from 2025-12-03

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