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6J36

crystal structure of Mycoplasma hyopneumoniae Enolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 501
ChainResidue
AALA421
AASN424
AARG425
AHOH616
AHOH619
BGLN22
BGLU393

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
AGLU393
AHOH620
BASN424
BARG425
AGLN22
AILE36

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 503
ChainResidue
APRO105
ALYS107
ATHR339
AASN340
AGLN362
AILE363

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 A 504
ChainResidue
AASN236
AGLY238
APHE239
ALYS240
AHIS455
AHIS456
AHIS457

site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 A 505
ChainResidue
AARG388
ASER389

site_idAC6
Number of Residues8
Detailsbinding site for residue GOL B 501
ChainResidue
BGLU47
BALA48
BPRO105
BASN106
BLYS107
BASN340
BILE363
BHOH613

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 B 502
ChainResidue
BASN236
BPHE239
BLYS240
BHIS455
BHIS456
BHIS457

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 B 503
ChainResidue
BLYS359
BARG388
BSER389

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKlNQIGTLSET
ChainResidueDetails
AILE356-THR369

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PDB entries from 2024-11-06

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