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4F4R

Crystal structure of D-mannonate dehydratase homolog from Chromohalobacter salexigens (Target EFI-502114), with bound NA, ordered loop

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0008927molecular_functionmannonate dehydratase activity
A0009063biological_processamino acid catabolic process
A0016052biological_processcarbohydrate catabolic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0047929molecular_functiongluconate dehydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP211
AGLU237
AASP238
AGLU263

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 502
ChainResidue
APRO80
APRO80
AVAL81
AVAL81

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
ATRP76
APRO171
AHIS313
APRO315
AASP317
AHOH710
AHOH941
AASN37

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 504
ChainResidue
AASP349
AHIS354
ATYR356
AHOH760

Functional Information from PROSITE/UniProt
site_idPS00908
Number of Residues26
DetailsMR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiAAVDmALwDIkAKaagmPLyqLLG
ChainResidueDetails
AALA85-GLY110

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the mutant P317A of D-mannonate dehydratase from Chromohalobacter salexigens complexed with Mg and D-Gluconate.","authors":["Fedorov A.A.","Fedorov E.V.","Wichelecki D.","Gerlt J.A.","Almo S.C."]}}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity"}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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