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3DFH

crystal structure of putative mandelate racemase / muconate lactonizing enzyme from Vibrionales bacterium SWAT-3

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
C0000287molecular_functionmagnesium ion binding
C0009063biological_processamino acid catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA C 501
ChainResidue
CSER249

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 502
ChainResidue
ASER249

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA B 503
ChainResidue
BSER249

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:24697546
ChainResidueDetails
AASP207
AGLU233
AGLU259
BASP207
BGLU233
BGLU259
CASP207
CGLU233
CGLU259

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:3SBF
ChainResidueDetails
AHIS209
CARG280
CHIS309
CGLU336
AARG280
AHIS309
AGLU336
BHIS209
BARG280
BHIS309
BGLU336
CHIS209

220113

PDB entries from 2024-05-22

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