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 | 0016829 | molecular_function | lyase activity |
| 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 | 0016829 | molecular_function | lyase activity |
| 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 |
