3V1K

Crystal Structure of the H265Q mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0009056	biological_process	catabolic process
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
A	0018771	molecular_function	2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity
A	0018774	molecular_function	2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity
A	0046464	biological_process	acylglycerol catabolic process
A	0047372	molecular_function	monoacylglycerol lipase activity
A	0070980	biological_process	biphenyl catabolic process
B	0003824	molecular_function	catalytic activity
B	0009056	biological_process	catabolic process
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016823	molecular_function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
B	0018771	molecular_function	2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity
B	0018774	molecular_function	2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity
B	0046464	biological_process	acylglycerol catabolic process
B	0047372	molecular_function	monoacylglycerol lipase activity
B	0070980	biological_process	biphenyl catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MLA A 287

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Transition state stabilizer