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1W6T

Crystal Structure Of Octameric Enolase From Streptococcus pneumoniae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0007155biological_processcell adhesion
A0009274cellular_componentpeptidoglycan-based cell wall
A0009986cellular_componentcell surface
A0016829molecular_functionlyase activity
A0042603cellular_componentcapsule
A0046872molecular_functionmetal ion binding
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0007155biological_processcell adhesion
B0009274cellular_componentpeptidoglycan-based cell wall
B0009986cellular_componentcell surface
B0016829molecular_functionlyase activity
B0042603cellular_componentcapsule
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 435
ChainResidue
AASP242
AGLU291
AASP318
AHOH2195
AHOH2204
AHOH2212

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 435
ChainResidue
BHOH2172
BHOH2173
BHOH2174
BASP242
BGLU291
BASP318

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 2PE A1434
ChainResidue
AGLU77
AALA78
AILE80

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 2PE B1434
ChainResidue
BGLU77
BALA78
BILE80
BGLY81
BTYR82
BHOH2259

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKvNQIGTLTET
ChainResidueDetails
AILE340-THR353

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLU205
BGLU205

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
ALYS343
BLYS343

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318
ChainResidueDetails
AGLN163
BLYS394
ALYS343
AARG372
ASER373
ALYS394
BGLN163
BLYS343
BARG372
BSER373

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15476816, ECO:0007744|PDB:1W6T
ChainResidueDetails
AASP242
AGLU291
AASP318
BASP242
BGLU291
BASP318

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AGLU164
AHIS371
ALYS394
AGLU205

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BGLU164
BHIS371
BLYS394
BGLU205

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AGLU164
ALYS343
AHIS371
AGLU205

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BGLU164
BLYS343
BHIS371
BGLU205

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
AHIS187
ALYS343

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1els
ChainResidueDetails
BHIS187
BLYS343

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PDB entries from 2024-07-24

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