1C8U

CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0006637	biological_process	acyl-CoA metabolic process
A	0009062	biological_process	fatty acid catabolic process
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0047617	molecular_function	fatty acyl-CoA hydrolase activity
A	0052815	molecular_function	medium-chain fatty acyl-CoA hydrolase activity
A	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
A	0141126	molecular_function	short-chain fatty acyl-CoA hydrolase activity
B	0005829	cellular_component	cytosol
B	0006637	biological_process	acyl-CoA metabolic process
B	0009062	biological_process	fatty acid catabolic process
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0047617	molecular_function	fatty acyl-CoA hydrolase activity
B	0052815	molecular_function	medium-chain fatty acyl-CoA hydrolase activity
B	0052816	molecular_function	long-chain fatty acyl-CoA hydrolase activity
B	0141126	molecular_function	short-chain fatty acyl-CoA hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LDA A 800

Chain	Residue
A	LEU31
A	PHE35
A	LEU220
A	HOH848
A	HOH874
A	HOH1010

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LDA B 801

Chain	Residue
B	HOH825
B	HOH847
B	HOH872
B	PHE219
B	LEU220
B	ILE226

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10876240","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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