6KA2
Crystal structure of a Thebaine synthase from Papaver somniferum in complex with TBN
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006952 | biological_process | defense response |
A | 0009820 | biological_process | alkaloid metabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016835 | molecular_function | carbon-oxygen lyase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0006952 | biological_process | defense response |
B | 0009820 | biological_process | alkaloid metabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016835 | molecular_function | carbon-oxygen lyase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
C | 0006952 | biological_process | defense response |
C | 0009820 | biological_process | alkaloid metabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0016835 | molecular_function | carbon-oxygen lyase activity |
C | 0042803 | molecular_function | protein homodimerization activity |
D | 0006952 | biological_process | defense response |
D | 0009820 | biological_process | alkaloid metabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0016835 | molecular_function | carbon-oxygen lyase activity |
D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue D4R A 200 |
Chain | Residue |
A | TRP63 |
A | HOH316 |
A | ILE72 |
A | SER74 |
A | HIS89 |
A | VAL91 |
A | PHE103 |
A | THR105 |
A | TYR139 |
A | PHE142 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue D4R B 200 |
Chain | Residue |
B | TRP63 |
B | VAL65 |
B | ILE72 |
B | SER74 |
B | THR105 |
B | ARG122 |
B | ILE124 |
B | TYR139 |
B | PHE142 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue D4R C 200 |
Chain | Residue |
C | TYR30 |
C | TRP63 |
C | SER74 |
C | HIS89 |
C | THR105 |
C | ARG122 |
C | SER123 |
C | ILE124 |
C | TYR139 |
C | HOH303 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:32703404, ECO:0007744|PDB:6KA3 |
Chain | Residue | Details |
A | HIS89 | |
B | HIS89 | |
C | HIS89 | |
D | HIS89 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32703404, ECO:0007744|PDB:6KA3 |
Chain | Residue | Details |
A | SER74 | |
A | THR105 | |
B | SER74 | |
B | THR105 | |
C | SER74 | |
C | THR105 | |
D | SER74 | |
D | THR105 |