5TIC
X-ray structure of wild-type E. coli Acyl-CoA thioesterase I at pH 5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004064 | molecular_function | arylesterase activity |
| A | 0004622 | molecular_function | lysophospholipase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0016297 | molecular_function | fatty acyl-[ACP] hydrolase activity |
| A | 0016298 | molecular_function | lipase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| A | 0052816 | molecular_function | long-chain fatty acyl-CoA hydrolase activity |
| A | 0102545 | molecular_function | phosphatidyl phospholipase B activity |
| B | 0004064 | molecular_function | arylesterase activity |
| B | 0004622 | molecular_function | lysophospholipase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0016297 | molecular_function | fatty acyl-[ACP] hydrolase activity |
| B | 0016298 | molecular_function | lipase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0047617 | molecular_function | fatty acyl-CoA hydrolase activity |
| B | 0052816 | molecular_function | long-chain fatty acyl-CoA hydrolase activity |
| B | 0102545 | molecular_function | phosphatidyl phospholipase B activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 201 |
| Chain | Residue |
| A | ARG108 |
| A | PHE139 |
Functional Information from PROSITE/UniProt
| site_id | PS01098 |
| Number of Residues | 11 |
| Details | LIPASE_GDSL_SER Lipolytic enzymes "G-D-S-L" family, serine active site. LLILGDSLs.AG |
| Chain | Residue | Details |
| A | LEU4-GLY14 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577, ECO:0000305|PubMed:8098033 |
| Chain | Residue | Details |
| A | SER10 | |
| B | SER10 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15697222, ECO:0000269|PubMed:16515533, ECO:0000305|PubMed:12842470, ECO:0000305|PubMed:12846577 |
| Chain | Residue | Details |
| A | ASP154 | |
| A | HIS157 | |
| B | ASP154 | |
| B | HIS157 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15697222 |
| Chain | Residue | Details |
| B | GLY44 | |
| B | ASN73 | |
| A | GLY44 | |
| A | ASN73 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 755 |
| Chain | Residue | Details |
| A | SER10 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY44 | electrostatic stabiliser |
| A | ASN73 | electrostatic stabiliser |
| A | ASP154 | electrostatic stabiliser, increase basicity |
| A | HIS157 | electrostatic stabiliser, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 755 |
| Chain | Residue | Details |
| B | HIS157 | electrostatic stabiliser, proton acceptor, proton donor |
| B | SER10 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLY44 | electrostatic stabiliser |
| B | ASN73 | electrostatic stabiliser |
| B | ASP154 | electrostatic stabiliser, increase basicity |
