1FC4
2-AMINO-3-KETOBUTYRATE COA LIGASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006567 | biological_process | 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 | 0003824 | molecular_function | catalytic activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006567 | biological_process | 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 | 6 |
Details | BINDING: in other chain |
Chain | Residue | Details |
A | CYS111 | |
A | ASP210 | |
A | THR241 | |
B | CYS111 | |
B | ASP210 | |
B | THR241 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:11318637 |
Chain | Residue | Details |
A | HIS136 | |
A | ARG368 | |
B | HIS136 | |
B | ARG368 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:11318637 |
Chain | Residue | Details |
A | SER185 | |
B | SER185 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | SER274 | |
B | SER274 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS244 | |
B | LYS244 |
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 | SER185 | electrostatic stabiliser, hydrogen bond donor |
A | HIS213 | proton acceptor, proton donor |
A | LYS244 | 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 | SER185 | electrostatic stabiliser, hydrogen bond donor |
B | HIS213 | proton acceptor, proton donor |
B | LYS244 | covalently attached, electron pair acceptor, electron pair donor, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |