2VBG
The complex structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis with 2R-1-hydroxyethyl-deazaThDP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0000949 | biological_process | aromatic amino acid family catabolic process to alcohol via Ehrlich pathway |
A | 0003824 | molecular_function | catalytic activity |
A | 0004737 | molecular_function | pyruvate decarboxylase activity |
A | 0005829 | cellular_component | cytosol |
A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0047433 | molecular_function | branched-chain-2-oxoacid decarboxylase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0000949 | biological_process | aromatic amino acid family catabolic process to alcohol via Ehrlich pathway |
B | 0003824 | molecular_function | catalytic activity |
B | 0004737 | molecular_function | pyruvate decarboxylase activity |
B | 0005829 | cellular_component | cytosol |
B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0047433 | molecular_function | branched-chain-2-oxoacid decarboxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A1548 |
Chain | Residue |
A | ASP429 |
A | ASN456 |
A | GLY458 |
A | R1T1549 |
A | HOH2367 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE R1T A1549 |
Chain | Residue |
A | ILE404 |
A | GLY428 |
A | ASP429 |
A | GLY430 |
A | SER431 |
A | ASN456 |
A | GLY458 |
A | TYR459 |
A | THR460 |
A | VAL461 |
A | GLU462 |
A | MG1548 |
A | HOH2327 |
A | HOH2367 |
A | HOH2477 |
A | HOH2478 |
B | PRO24 |
B | GLY25 |
B | GLU49 |
B | VAL74 |
B | HIS113 |
A | GLY378 |
A | THR379 |
A | GLY402 |
A | SER403 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B1548 |
Chain | Residue |
B | ASP429 |
B | ASN456 |
B | GLY458 |
B | R1T1549 |
B | HOH2374 |
site_id | AC4 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE R1T B1549 |
Chain | Residue |
A | PRO24 |
A | GLY25 |
A | GLU49 |
A | VAL74 |
A | HIS113 |
B | GLY378 |
B | THR379 |
B | GLY402 |
B | SER403 |
B | ILE404 |
B | GLY428 |
B | ASP429 |
B | GLY430 |
B | SER431 |
B | ASN456 |
B | GLY458 |
B | TYR459 |
B | THR460 |
B | VAL461 |
B | GLU462 |
B | MG1548 |
B | HOH2374 |
B | HOH2471 |
B | HOH2472 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pvd |
Chain | Residue | Details |
A | HIS113 | |
A | GLU462 | |
A | HIS112 | |
A | ASP26 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1pvd |
Chain | Residue | Details |
B | HIS113 | |
B | GLU462 | |
B | HIS112 | |
B | ASP26 |