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3RR1

Crystal structure of enolase PRK14017 (target EFI-500653) from Ralstonia pickettii 12J

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008869molecular_functiongalactonate dehydratase activity
A0009063biological_processamino acid catabolic process
A0016829molecular_functionlyase activity
A0034194biological_processD-galactonate catabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0008869molecular_functiongalactonate dehydratase activity
B0009063biological_processamino acid catabolic process
B0016829molecular_functionlyase activity
B0034194biological_processD-galactonate catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 405
ChainResidue
AGLY76
AILE78
ALEU79
BCL405

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 405
ChainResidue
ACL405
BGLY75
BGLY76
BILE78
BLEU79

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLT B 406
ChainResidue
BLYS194
BALA221
BARG222
BALA224
BALA225
BHIS226
BALA249
BGLY250
BGLY251
BHOH470

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiAGIDqALwDIkGKvlgvPVyeLLG
ChainResidueDetails
AALA82-GLY107

site_idPS00909
Number of Residues32
DetailsMR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. FglDfHgrvsapmAkvlikeLepyrplfIEEP
ChainResidueDetails
APHE180-PRO211

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS185
BHIS185

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS285
BHIS285

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01289
ChainResidueDetails
AASP183
AGLU209
AGLU235
BASP183
BGLU209
BGLU235

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Increases basicity of active site His => ECO:0000255|HAMAP-Rule:MF_01289
ChainResidueDetails
AASP258
BASP258

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01289
ChainResidueDetails
AGLU310
BGLU310

226707

PDB entries from 2024-10-30

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