1FC4
2-AMINO-3-KETOBUTYRATE COA LIGASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006567 | biological_process | L-threonine catabolic process |
| A | 0008890 | molecular_function | glycine C-acetyltransferase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0019518 | biological_process | L-threonine catabolic process to glycine |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006567 | biological_process | L-threonine catabolic process |
| B | 0008890 | molecular_function | glycine C-acetyltransferase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0019518 | biological_process | L-threonine catabolic process to glycine |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AKB A 1200 |
| Chain | Residue |
| A | ASN50 |
| A | HOH1705 |
| B | VAL79 |
| B | ILE82 |
| B | HOH1254 |
| A | HIS136 |
| A | SER185 |
| A | MSE186 |
| A | HIS213 |
| A | LYS244 |
| A | ARG368 |
| A | PLP1201 |
| A | HOH1253 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 1201 |
| Chain | Residue |
| A | SER110 |
| A | CYS111 |
| A | PHE112 |
| A | HIS136 |
| A | ASP181 |
| A | SER185 |
| A | ASP210 |
| A | SER212 |
| A | HIS213 |
| A | THR241 |
| A | LYS244 |
| A | AKB1200 |
| A | HOH1278 |
| A | HOH1705 |
| B | PHE273 |
| B | SER274 |
| B | ASN275 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AKB B 1202 |
| Chain | Residue |
| A | ILE82 |
| A | HOH1212 |
| B | ASN50 |
| B | HIS136 |
| B | SER185 |
| B | MSE186 |
| B | HIS213 |
| B | LYS244 |
| B | ARG368 |
| B | PLP1203 |
| B | HOH1259 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 1203 |
| Chain | Residue |
| A | PHE273 |
| A | SER274 |
| A | ASN275 |
| B | SER110 |
| B | CYS111 |
| B | PHE112 |
| B | HIS136 |
| B | ASP181 |
| B | SER185 |
| B | ASP210 |
| B | SER212 |
| B | HIS213 |
| B | THR241 |
| B | LYS244 |
| B | GLY251 |
| B | AKB1202 |
| B | HOH1315 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLGKALGGAS |
| Chain | Residue | Details |
| A | THR241-SER250 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"description":"in other chain"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00985","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11318637","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00985","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11318637","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11318637 |
| Chain | Residue | Details |
| A | HIS213 | |
| A | LYS244 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11318637 |
| Chain | Residue | Details |
| B | HIS213 | |
| B | LYS244 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 762 |
| Chain | Residue | Details |
| A | ALA205 | electrostatic stabiliser, hydrogen bond donor |
| A | THR241 | proton acceptor, proton donor |
| A | SER276 | covalently attached, electron pair acceptor, electron pair donor, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 762 |
| Chain | Residue | Details |
| B | ALA205 | electrostatic stabiliser, hydrogen bond donor |
| B | THR241 | proton acceptor, proton donor |
| B | SER276 | covalently attached, electron pair acceptor, electron pair donor, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
