1I2K
AMINODEOXYCHORISMATE LYASE FROM ESCHERICHIA COLI
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005829 | cellular_component | cytosol |
A | 0008153 | biological_process | para-aminobenzoic acid biosynthetic process |
A | 0008696 | molecular_function | 4-amino-4-deoxychorismate lyase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0046394 | biological_process | carboxylic acid biosynthetic process |
A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
A | 0046656 | biological_process | folic acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP A 301 |
Chain | Residue |
A | ARG45 |
A | GLY199 |
A | ILE200 |
A | MET201 |
A | ASN236 |
A | ALA237 |
A | HOH413 |
A | HOH576 |
A | HOH577 |
A | TYR92 |
A | LYS140 |
A | GLU173 |
A | CYS175 |
A | ALA176 |
A | ALA177 |
A | ASN178 |
A | VAL197 |
Functional Information from PROSITE/UniProt
site_id | PS00770 |
Number of Residues | 30 |
Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EcCaaNLFwrkgnv......VyTprldqag.VnGImR |
Chain | Residue | Details |
A | GLU173-ARG202 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS140 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
A | LYS140 | |
A | VAL197 | |
A | GLU173 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
A | ILE139 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1daa |
Chain | Residue | Details |
A | HIS141 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 305 |
Chain | Residue | Details |
A | THR28 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | LYS140 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | GLU173 | electrostatic stabiliser, hydrogen bond acceptor |