2H9C
Native Crystal Structure of the Isochorismate-Pyruvate Lyase from Pseudomonas aeruginosa
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 | 6 |
Details | BINDING SITE FOR RESIDUE NO3 A 100 |
Chain | Residue |
A | ARG31 |
A | ARG53 |
A | MET57 |
A | ILE83 |
A | TYR86 |
B | ILE17 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 B 100 |
Chain | Residue |
B | HOH101 |
B | ARG31 |
B | PRO49 |
B | MET57 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NO3 A 101 |
Chain | Residue |
A | GLN26 |
B | GLY9 |
B | ALA11 |
B | ASP12 |
B | GLU67 |
B | ASN68 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NO3 A 102 |
Chain | Residue |
A | LYS36 |
A | ALA37 |
A | ARG40 |
A | HOH120 |
B | PRO4 |
B | GLU5 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 A 103 |
Chain | Residue |
A | GLN26 |
A | ARG30 |
B | LYS2 |
B | THR8 |
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 | LYS42 | |
B | ARG14 | |
B | LYS42 |
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 | 2 |
Details | Annotated By Reference To The Literature 1ecm |
Chain | Residue | Details |
A | ARG14 | |
B | ARG31 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ecm |
Chain | Residue | Details |
A | ARG31 | |
B | ARG14 |