1CSM
THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION
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 | tyrosine biosynthetic process |
A | 0008152 | biological_process | metabolic 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 |
B | 0003824 | molecular_function | catalytic activity |
B | 0004106 | molecular_function | chorismate mutase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0006571 | biological_process | tyrosine biosynthetic process |
B | 0008152 | biological_process | metabolic process |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0009094 | biological_process | L-phenylalanine biosynthetic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0046417 | biological_process | chorismate metabolic process |
B | 0072545 | molecular_function | L-tyrosine binding |
B | 0120284 | molecular_function | tryptophan binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRP B 501 |
Chain | Residue |
A | ILE74 |
A | ARG76 |
A | GLU82 |
B | ASN138 |
B | ASN139 |
B | PHE140 |
B | GLY141 |
B | SER142 |
B | HOH516 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE TRP A 502 |
Chain | Residue |
A | ASN138 |
A | ASN139 |
A | PHE140 |
A | GLY141 |
A | SER142 |
A | THR145 |
A | HOH527 |
A | HOH536 |
A | HOH563 |
A | HOH574 |
B | ILE74 |
B | ARG76 |
B | GLU82 |
B | HOH521 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8622937, ECO:0007744|PDB:2CSM |
Chain | Residue | Details |
A | ARG75 | |
B | GLY141 | |
B | SER142 | |
B | THR145 | |
A | ARG76 | |
A | ASN139 | |
A | GLY141 | |
A | SER142 | |
A | THR145 | |
B | ARG75 | |
B | ARG76 | |
B | ASN139 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7971967, ECO:0007744|PDB:1CSM |
Chain | Residue | Details |
A | ASN138 | |
B | ASN138 |
Catalytic Information from CSA
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 |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 81 |
Chain | Residue | Details |
B | ARG16 | hydrogen bond donor, transition state stabiliser |
B | ARG157 | hydrogen bond donor, transition state stabiliser |
B | LYS168 | hydrogen bond donor, transition state stabiliser |
B | ASN194 | transition state stabiliser |
B | GLU198 | hydrogen bond acceptor, transition state stabiliser |
B | THR242 | transition state stabiliser |
B | GLU246 | hydrogen bond donor, transition state stabiliser |