4DI9

CRYSTAL STRUCTURE OF THE D248A mutant of 2-PYRONE-4,6-DICARBOXYLIC ACID HYDROLASE FROM SPHINGOMONAS PAUCIMOBILIS complexed with substrate at pH 6.5

Replaces:  4D9A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009056	biological_process	catabolic process
A	0016787	molecular_function	hydrolase activity
A	0019619	biological_process	3,4-dihydroxybenzoate catabolic process
A	0046274	biological_process	lignin catabolic process
A	0047554	molecular_function	2-pyrone-4,6-dicarboxylate lactonase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 0GY A 401

Chain	Residue
A	HIS31
A	HIS180
A	ARG183
A	ARG217
A	PRO252
A	ASN253
A	ACT402
A	HOH653
A	HIS33
A	TYR49
A	ALA76
A	SER77
A	ARG124
A	ARG130
A	LEU131
A	TYR156

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT A 402

Chain	Residue
A	ARG130
A	ARG183
A	ARG217
A	ASN253
A	0GY401
A	HOH573
A	HOH744

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:22475079

Chain	Residue	Details
A	ALA248

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:22475079

Chain	Residue	Details
A	HIS31
A	TYR49
A	SER77
A	ARG124
A	ARG130
A	TYR156
A	HIS180
A	ASN253

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