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2PMQ

Crystal structure of a mandelate racemase/muconate lactonizing enzyme from Roseovarius sp. HTCC2601

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0006579biological_processamino-acid betaine catabolic process
A0016853molecular_functionisomerase activity
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0046872molecular_functionmetal ion binding
A0047661molecular_functionamino-acid racemase activity
B0000287molecular_functionmagnesium ion binding
B0006579biological_processamino-acid betaine catabolic process
B0016853molecular_functionisomerase activity
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0046872molecular_functionmetal ion binding
B0047661molecular_functionamino-acid racemase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 901
ChainResidue
AHOH1056
AHOH1250
AHOH1258
BHOH1038
BHOH1074
BHOH1163

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 902
ChainResidue
AASP241
AHOH913
AHOH965
AHOH1239
AASP193
AASN195
AGLU218

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MG A 903
ChainResidue
AHIS235
AHIS235
AHIS235
AHIS235
AHOH945
AHOH945
AHOH945
AHOH945
AHOH1118
AHOH1118
AHOH1118
AHOH1118

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 904
ChainResidue
BASP193
BGLU218
BASP241
BHOH921
BHOH933
BHOH1005

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MG B 905
ChainResidue
BHIS235
BHIS235
BHIS235
BHIS235
BHOH963
BHOH963
BHOH963
BHOH963
BHOH1134
BHOH1134
BHOH1134
BHOH1134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
ALYS265
ALYS163

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1r6w
ChainResidueDetails
BLYS265
BLYS163

site_idMCSA1
Number of Residues6
DetailsM-CSA 940
ChainResidueDetails
AALA175proton shuttle (general acid/base)
AARG205metal ligand
ACYS234metal ligand
AGLY261metal ligand
AHIS289proton shuttle (general acid/base)
AGLY352electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 940
ChainResidueDetails
BALA175proton shuttle (general acid/base)
BARG205metal ligand
BCYS234metal ligand
BGLY261metal ligand
BHIS289proton shuttle (general acid/base)
BGLY352electrostatic stabiliser

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PDB entries from 2025-10-15

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