3HGX
Crystal Structure of Pseudomonas aeruginosa Isochorismate-Pyruvate Lyase K42A mutant in complex with salicylate and pyruvate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004106 | molecular_function | chorismate mutase activity |
A | 0009697 | biological_process | salicylic acid biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016835 | molecular_function | carbon-oxygen lyase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0042864 | biological_process | pyochelin biosynthetic process |
A | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
A | 0046417 | biological_process | chorismate metabolic process |
B | 0004106 | molecular_function | chorismate mutase activity |
B | 0009697 | biological_process | salicylic acid biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016835 | molecular_function | carbon-oxygen lyase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0042864 | biological_process | pyochelin biosynthetic process |
B | 0043904 | molecular_function | isochorismate pyruvate lyase activity |
B | 0046417 | biological_process | chorismate metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SAL A 101 |
Chain | Residue |
A | ARG31 |
B | HOH107 |
A | VAL35 |
A | ILE48 |
A | PRO49 |
A | MET57 |
A | TYR86 |
A | ILE87 |
A | GLN90 |
B | PYR102 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PYR B 102 |
Chain | Residue |
A | ALA38 |
A | ARG53 |
A | GLN90 |
B | ARG14 |
B | HOH107 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PYR A 103 |
Chain | Residue |
A | ARG14 |
A | ILE17 |
B | ALA38 |
B | ARG53 |
B | GLN90 |
B | SAL104 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SAL B 104 |
Chain | Residue |
A | PYR103 |
B | ARG31 |
B | VAL35 |
B | ILE48 |
B | PRO49 |
B | MET57 |
B | TYR86 |
B | ILE87 |
B | GLN90 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:21751784 |
Chain | Residue | Details |
A | ARG14 | |
A | ALA42 | |
B | ARG14 | |
B | ALA42 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16914555, ECO:0000269|PubMed:19432488, ECO:0000269|PubMed:21751784 |
Chain | Residue | Details |
A | ARG31 | |
A | GLN90 | |
B | ARG31 | |
B | GLN90 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ecm |
Chain | Residue | Details |
A | ARG31 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ecm |
Chain | Residue | Details |
B | ARG31 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ecm |
Chain | Residue | Details |
A | ARG14 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ecm |
Chain | Residue | Details |
B | ARG14 |