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3BJS

Crystal structure of a member of enolase superfamily from Polaromonas sp. JS666

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016836molecular_functionhydro-lyase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0009063biological_processamino acid catabolic process
B0016052biological_processcarbohydrate catabolic process
B0016836molecular_functionhydro-lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
ALYS203
AASP233
AGLU259
AGLU286

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 501
ChainResidue
BLYS203
BASP233
BGLU259
BGLU286

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiSGIDmALwDIrGKaanmPLyeLLG
ChainResidueDetails
AALA139-GLY164

site_idPS00909
Number of Residues32
DetailsMR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. IltDaNtaytmadArrvlpvLaeiqagwLEEP
ChainResidueDetails
AILE230-PRO261

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PDB entries from 2025-07-30

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