3RP7

Crystal Structure of Klebsiella pneumoniae HpxO complexed with FAD and uric acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0004846	molecular_function	urate oxidase activity
A	0006144	biological_process	purine nucleobase metabolic process
A	0016709	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
A	0019628	biological_process	urate catabolic process
A	0071949	molecular_function	FAD binding
A	0102099	molecular_function	FAD-dependent urate hydroxylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE URC A 7579

Chain	Residue
A	SER43
A	HOH401
A	HOH473
A	ASN178
A	ARG204
A	TYR216
A	PHE218
A	PRO292
A	ASP293
A	GLY295
A	FAD385

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site_id	AC2
Number of Residues	34
Details	BINDING SITE FOR RESIDUE FAD A 385

Chain	Residue
A	ILE6
A	GLY7
A	GLY9
A	ILE10
A	GLY11
A	GLU30
A	ALA31
A	VAL32
A	ILE42
A	SER43
A	ARG103
A	LYS123
A	ARG124
A	VAL125
A	ALA153
A	ASP154
A	GLY155
A	GLY284
A	ASP285
A	PRO292
A	GLY295
A	GLN296
A	GLY297
A	GLY298
A	CYS299
A	HOH386
A	HOH387
A	HOH395
A	HOH406
A	HOH474
A	HOH494
A	HOH522
A	HOH554
A	URC7579

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:23259842, ECO:0007744|PDB:3RP6, ECO:0007744|PDB:3RP7, ECO:0007744|PDB:3RP8

Chain	Residue	Details
A	GLY11
A	GLU30
A	SER43
A	VAL125
A	ASP285
A	GLY295

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:23259842, ECO:0007744|PDB:3RP7

Chain	Residue	Details
A	ASN178
A	ARG204
A	TYR216

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Involved in substrate activation for the transfer of oxygen from the flavin hydroperoxide => ECO:0000305|PubMed:23259842

Chain	Residue	Details
A	ARG204

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