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4DI8

CRYSTAL STRUCTURE OF THE D248A mutant of 2-PYRONE-4,6-DICARBOXYLIC ACID HYDROLASE FROM SPHINGOMONAS PAUCIMOBILIS complexed with substrate at pH 8.5

Replaces:  4D95
Functional Information from GO Data
ChainGOidnamespacecontents
A0009056biological_processcatabolic process
A0016787molecular_functionhydrolase activity
A0019619biological_process3,4-dihydroxybenzoate catabolic process
A0046274biological_processlignin catabolic process
A0047554molecular_function2-pyrone-4,6-dicarboxylate lactonase activity
B0009056biological_processcatabolic process
B0016787molecular_functionhydrolase activity
B0019619biological_process3,4-dihydroxybenzoate catabolic process
B0046274biological_processlignin catabolic process
B0047554molecular_function2-pyrone-4,6-dicarboxylate lactonase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 0GZ A 401
ChainResidue
AHIS31
AHIS180
AARG183
AARG217
AASN253
AACT402
AHIS33
ATYR49
AALA76
ASER77
AARG124
AARG130
ALEU131
ATYR156

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT A 402
ChainResidue
AARG130
AARG183
AARG217
AASN253
A0GZ401
A0GY403
AHOH651
AHOH705

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 0GY A 403
ChainResidue
AHIS31
AHIS33
ATYR49
AALA76
ASER77
AARG124
AARG130
ALEU131
ATYR156
AHIS180
AARG183
AARG217
APRO252
AASN253
AACT402

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 0GZ B 401
ChainResidue
BHIS31
BHIS33
BTYR49
BSER77
BARG124
BARG130
BLEU131
BTYR156
BHIS180
BARG183
BARG217
BPRO252
BASN253
BACT402
BHOH698

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 402
ChainResidue
BARG130
BARG183
BARG217
BASN253
B0GY405
BHOH735
BHOH826

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 403
ChainResidue
BHOH591
BHOH688
BHOH701
BHOH741
BHOH759
BHOH783

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 404
ChainResidue
BHOH630
BHOH674
BHOH719
BHOH737
BHOH781

site_idAC8
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0GY B 405
ChainResidue
BHIS31
BHIS33
BTYR49
BALA76
BSER77
BARG124
BARG130
BLEU131
BTYR156
BHIS180
BARG183
BARG217
BPRO252
BASN253
BACT402
BHOH698

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:22475079
ChainResidueDetails
AALA248
BALA248

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:22475079
ChainResidueDetails
AHIS31
BTYR49
BSER77
BARG124
BARG130
BTYR156
BHIS180
BASN253
ATYR49
ASER77
AARG124
AARG130
ATYR156
AHIS180
AASN253
BHIS31

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PDB entries from 2024-11-06

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