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3S47

Crystal structure of enolase superfamily member from Clostridium beijerincki complexed with Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009063biological_processamino acid catabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0009063biological_processamino acid catabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AASP207
AGLU233
AGLU259
AARG280
AHOH432
AHOH551

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BHOH434
BHOH565
BHOH566
BASP207
BGLU233
BGLU259

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiSGVDmALwDIkGKlanmPLyqLFG
ChainResidueDetails
AALA91-GLY116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24697546","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of putative mandelate racemase/muconate lactonizing protein from Clostridium beijerinckii NCIMB 8052.","authoringGroup":["New York structural genomix research consortium (NYSGXRC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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