6PCD
Crystal structure of beta-ketoadipyl-CoA thiolase mutant (C90S-H356A) in complex Octanoyl coenzyme A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
A | 0033812 | molecular_function | 3-oxoadipyl-CoA thiolase activity |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
B | 0033812 | molecular_function | 3-oxoadipyl-CoA thiolase activity |
C | 0016746 | molecular_function | acyltransferase activity |
C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
C | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
C | 0033812 | molecular_function | 3-oxoadipyl-CoA thiolase activity |
D | 0016746 | molecular_function | acyltransferase activity |
D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
D | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
D | 0033812 | molecular_function | 3-oxoadipyl-CoA thiolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue COA A 501 |
Chain | Residue |
A | SER90 |
A | ASN322 |
A | ALA356 |
A | HOH622 |
A | HOH724 |
A | HOH742 |
A | HOH817 |
A | HOH845 |
A | HOH849 |
A | ILE145 |
A | MET163 |
A | ARG226 |
A | THR229 |
A | ALA249 |
A | GLY250 |
A | SER253 |
A | GLY254 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue OYA A 502 |
Chain | Residue |
A | ASN58 |
A | THR143 |
A | THR144 |
A | GLY146 |
A | ARG148 |
A | MET163 |
A | LEU358 |
A | HOH603 |
A | HOH880 |
D | ARG65 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | ARG187 |
A | SER188 |
A | LYS191 |
A | GLU323 |
A | VAL345 |
A | ASN346 |
A | GLY349 |
A | HOH640 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue CL A 504 |
Chain | Residue |
A | ASN322 |
A | ARG364 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue OYA B 501 |
Chain | Residue |
B | ASN58 |
B | THR143 |
B | THR144 |
B | ILE145 |
B | GLY146 |
B | ARG148 |
B | LEU358 |
B | HOH607 |
B | HOH875 |
C | ARG65 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | ARG187 |
B | SER188 |
B | LYS191 |
B | GLU323 |
B | ASP341 |
B | VAL345 |
B | ASN346 |
B | GLY349 |
B | HOH610 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CL B 503 |
Chain | Residue |
B | ASN322 |
B | ARG364 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue CL B 504 |
Chain | Residue |
B | ARG65 |
C | GLY146 |
C | GOL502 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue K B 505 |
Chain | Residue |
B | ALA9 |
B | ARG40 |
B | GLU203 |
B | HOH922 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue GOL C 501 |
Chain | Residue |
C | ARG187 |
C | SER188 |
C | LYS191 |
C | GLU323 |
C | VAL345 |
C | ASN346 |
C | GLY349 |
C | HOH630 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue GOL C 502 |
Chain | Residue |
B | ARG65 |
B | CL504 |
C | ALA57 |
C | ASN58 |
C | THR143 |
C | THR144 |
C | ARG148 |
C | LEU358 |
C | HOH749 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CL C 503 |
Chain | Residue |
C | ASN322 |
C | ARG364 |
C | LEU365 |
C | HOH823 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue K C 504 |
Chain | Residue |
B | PHE53 |
B | HOH706 |
C | ARG88 |
C | ASP95 |
C | THR99 |
C | HOH784 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue K C 505 |
Chain | Residue |
C | ARG136 |
C | MET138 |
D | HOH861 |
site_id | AD6 |
Number of Residues | 18 |
Details | binding site for residue COA D 501 |
Chain | Residue |
D | THR229 |
D | ALA249 |
D | GLY250 |
D | SER253 |
D | GLY254 |
D | ASN322 |
D | ALA324 |
D | HOH607 |
D | HOH676 |
D | HOH687 |
D | HOH725 |
D | HOH731 |
D | HOH860 |
D | HOH894 |
D | SER90 |
D | ILE145 |
D | MET163 |
D | ARG226 |
site_id | AD7 |
Number of Residues | 9 |
Details | binding site for residue OYA D 502 |
Chain | Residue |
A | ARG65 |
D | ALA57 |
D | ASN58 |
D | THR143 |
D | THR144 |
D | GLY146 |
D | ARG148 |
D | LEU358 |
D | HOH916 |
site_id | AD8 |
Number of Residues | 8 |
Details | binding site for residue GOL D 503 |
Chain | Residue |
D | ARG187 |
D | SER188 |
D | LYS191 |
D | GLU323 |
D | VAL345 |
D | ASN346 |
D | GLY349 |
D | HOH639 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue CL D 504 |
Chain | Residue |
D | ASN322 |
D | ARG364 |
D | HOH823 |
Functional Information from PROSITE/UniProt
site_id | PS00099 |
Number of Residues | 14 |
Details | THIOLASE_3 Thiolases active site. GLATMCVGvGqGlA |
Chain | Residue | Details |
A | GLY381-ALA394 |