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3GY1

CRYSTAL STRUCTURE OF putative mandelate racemase/muconate lactonizing protein from Clostridium beijerinckii NCIMB 8052

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 500
ChainResidue
AASP207
AGLU233
AGLU259
BHOH509
BHOH545
BHOH746

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 500
ChainResidue
BHOH495
BHOH611
BHOH655
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: BINDING => ECO:0000269|PubMed:24697546, ECO:0000269|Ref.2
ChainResidueDetails
AASP207
AGLU233
AGLU259
BASP207
BGLU233
BGLU259

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS209
AARG280
AHIS309
AGLU336
BHIS209
BARG280
BHIS309
BGLU336

221051

PDB entries from 2024-06-12

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