1NL7
Z. ramigera biosynthetic thiolase, acetylated enzyme complexed with CoA at pH 9.5
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
B | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
C | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0016746 | molecular_function | acyltransferase activity |
C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
C | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
D | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0016746 | molecular_function | acyltransferase activity |
D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
D | 0042619 | biological_process | poly-hydroxybutyrate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 9720 |
Chain | Residue |
A | SER260 |
A | ALA262 |
A | ARG266 |
A | HOH9957 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 9722 |
Chain | Residue |
A | HOH9849 |
A | LYS298 |
A | ARG302 |
A | HOH470 |
A | HOH537 |
A | HOH538 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE COA A 1393 |
Chain | Residue |
A | SCY89 |
A | LEU148 |
A | HIS156 |
A | MET157 |
A | SER227 |
A | ALA243 |
A | GLY244 |
A | SER247 |
A | MET288 |
A | PHE319 |
A | HIS348 |
A | HOH409 |
A | HOH481 |
A | HOH498 |
A | HOH513 |
A | HOH532 |
A | HOH554 |
A | HOH9804 |
A | HOH9858 |
C | LYS208 |
D | MET134 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 9719 |
Chain | Residue |
B | LYS298 |
B | ARG302 |
B | HOH540 |
B | HOH9928 |
B | HOH9931 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 9721 |
Chain | Residue |
B | SER260 |
B | ARG266 |
B | HOH419 |
B | HOH9883 |
B | HOH9952 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE COA B 5939 |
Chain | Residue |
B | SCY89 |
B | LEU148 |
B | HIS156 |
B | MET157 |
B | ARG220 |
B | SER227 |
B | MET228 |
B | LEU231 |
B | GLY244 |
B | SER247 |
B | MET288 |
B | ALA318 |
B | PHE319 |
B | HIS348 |
B | HOH467 |
B | HOH534 |
B | HOH9824 |
B | HOH9834 |
B | HOH9900 |
B | HOH9919 |
Functional Information from PROSITE/UniProt
site_id | PS00098 |
Number of Residues | 19 |
Details | THIOLASE_1 Thiolases acyl-enzyme intermediate signature. MNQlCGSGLrAValgmqqI |
Chain | Residue | Details |
A | MET85-ILE103 |
site_id | PS00099 |
Number of Residues | 14 |
Details | THIOLASE_3 Thiolases active site. GLATLCIGgGmGvA |
Chain | Residue | Details |
A | GLY373-ALA386 |
site_id | PS00737 |
Number of Residues | 17 |
Details | THIOLASE_2 Thiolases signature 2. NvnGGaIAiGHPiGaSG |
Chain | Residue | Details |
A | ASN338-GLY354 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Acyl-thioester intermediate |
Chain | Residue | Details |
A | SCY89 | |
B | SCY89 | |
C | SCY89 | |
D | SCY89 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS348 | |
A | CYS378 | |
B | HIS348 | |
B | CYS378 | |
C | HIS348 | |
C | CYS378 | |
D | HIS348 | |
D | CYS378 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
A | HIS348 | |
A | GLY380 | |
A | CYS378 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
B | HIS348 | |
B | GLY380 | |
B | CYS378 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
C | HIS348 | |
C | GLY380 | |
C | CYS378 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
D | HIS348 | |
D | GLY380 | |
D | CYS378 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
A | HIS348 | |
A | CYS378 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
B | HIS348 | |
B | CYS378 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
C | HIS348 | |
C | CYS378 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1afw |
Chain | Residue | Details |
D | HIS348 | |
D | CYS378 |