2CSM
TYR-BOUND T-STATE OF YEAST CHORISMATE MUTASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | tyrosine 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: BINDING => ECO:0000269|PubMed:8622937, ECO:0007744|PDB:2CSM |
Chain | Residue | Details |
A | ARG75 | |
A | ARG76 | |
A | ASN139 | |
A | GLY141 | |
A | SER142 | |
A | THR145 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7971967, ECO:0007744|PDB:1CSM |
Chain | Residue | Details |
A | ASN138 |
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 |