2CSM
TYR-BOUND T-STATE OF YEAST CHORISMATE MUTASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004106 | molecular_function | chorismate mutase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006571 | biological_process | L-tyrosine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009094 | biological_process | L-phenylalanine biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046417 | biological_process | chorismate metabolic process |
| A | 0072545 | molecular_function | L-tyrosine binding |
| A | 0120284 | molecular_function | tryptophan binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TYR A 300 |
| Chain | Residue |
| A | ILE74 |
| A | ARG75 |
| A | ARG76 |
| A | ASN139 |
| A | GLY141 |
| A | SER142 |
| A | THR145 |
| site_id | CAT |
| Number of Residues | 7 |
| Details | PRESUMED CATALYTIC SITE. |
| Chain | Residue |
| A | ASN194 |
| A | GLU198 |
| A | GLU246 |
| A | THR242 |
| A | ARG157 |
| A | ARG16 |
| A | LYS168 |
| site_id | REG |
| Number of Residues | 7 |
| Details | REGULATORY, ALLOSTERIC SITE. ONLY POLAR CONTACTS TO TYR ARE LISTED. RESIDUES 138 - 145 MUST BE TRANSFORMED TO GENERATE THE SECOND SUBUNIT OF THE DIMER IN ORDER TO BUILD A COMPLETE REGULATORY SITE. |
| Chain | Residue |
| A | ASN138 |
| A | ASN139 |
| A | GLY141 |
| A | SER142 |
| A | THR145 |
| A | ARG75 |
| A | ARG76 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8622937","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CSM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7971967","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CSM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3csm |
| Chain | Residue | Details |
| A | GLU246 | |
| A | ARG16 | |
| A | ARG157 | |
| A | LYS168 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 81 |
| Chain | Residue | Details |
| A | ARG16 | hydrogen bond donor, transition state stabiliser |
| A | ARG157 | hydrogen bond donor, transition state stabiliser |
| A | LYS168 | hydrogen bond donor, transition state stabiliser |
| A | ASN194 | transition state stabiliser |
| A | GLU198 | hydrogen bond acceptor, transition state stabiliser |
| A | THR242 | transition state stabiliser |
| A | GLU246 | hydrogen bond donor, transition state stabiliser |
