Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0003984 | molecular_function | acetolactate synthase activity |
A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 699 |
Chain | Residue |
A | ASP538 |
A | ASN565 |
A | HIS567 |
A | TPP702 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 1IQ A 694 |
Chain | Residue |
A | PRO281 |
A | ILE396 |
A | ASP397 |
A | NHE696 |
A | HOH4032 |
A | HOH4149 |
A | LYS220 |
A | GLY245 |
A | ARG246 |
A | TYR276 |
A | ARG279 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 1IQ A 695 |
Chain | Residue |
A | GLY121 |
A | ALA122 |
A | SER168 |
A | ARG199 |
A | MET200 |
A | PHE206 |
A | GLN207 |
A | LYS256 |
A | MET351 |
A | ASP376 |
A | ARG377 |
A | TRP574 |
A | SER653 |
A | GLY654 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE NHE A 696 |
Chain | Residue |
A | LYS220 |
A | HIS221 |
A | MET226 |
A | ARG272 |
A | LEU273 |
A | PRO274 |
A | GLY275 |
A | TYR276 |
A | 1IQ694 |
site_id | AC5 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD A 701 |
Chain | Residue |
A | PHE206 |
A | ARG246 |
A | GLY307 |
A | GLY308 |
A | GLY309 |
A | THR331 |
A | LEU332 |
A | MET333 |
A | LEU349 |
A | GLY350 |
A | MET351 |
A | HIS352 |
A | GLY371 |
A | VAL372 |
A | ARG373 |
A | ASP375 |
A | ARG377 |
A | VAL378 |
A | ASP395 |
A | ILE396 |
A | GLU400 |
A | GLY413 |
A | ASP414 |
A | VAL415 |
A | GLN489 |
A | MET490 |
A | GLY508 |
A | GLY509 |
A | HOH4030 |
A | HOH4182 |
A | HOH4218 |
A | HOH4219 |
A | HOH4258 |
site_id | AC6 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE TPP A 702 |
Chain | Residue |
A | TYR118 |
A | PRO119 |
A | GLY120 |
A | GLU144 |
A | PRO170 |
A | ASN174 |
A | GLN207 |
A | VAL485 |
A | GLY486 |
A | GLN487 |
A | HIS488 |
A | GLY511 |
A | MET513 |
A | GLY537 |
A | ASP538 |
A | GLY539 |
A | SER540 |
A | ASN565 |
A | HIS567 |
A | LEU568 |
A | GLY569 |
A | MET570 |
A | VAL571 |
A | MG699 |
A | HOH4108 |
Functional Information from PROSITE/UniProt
site_id | PS00187 |
Number of Residues | 20 |
Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGasvanPdaivVdIdGDGS |
Chain | Residue | Details |
A | ILE521-SER540 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU144 | |
A | GLN207 | |
A | ARG246 | |
A | ASP414 | |
Chain | Residue | Details |
A | SER186 | |
A | GLN487 | |
Chain | Residue | Details |
A | LYS220 | |
Chain | Residue | Details |
A | LYS256 | |
A | ASP376 | |
A | TRP574 | |
A | SER653 | |
Chain | Residue | Details |
A | GLY308 | |
A | THR331 | |
A | LEU349 | |
A | GLY371 | |
A | ASP395 | |
A | GLY508 | |
Chain | Residue | Details |
A | GLY511 | |
Chain | Residue | Details |
A | ASP538 | |
Chain | Residue | Details |
A | ASN565 | |
Chain | Residue | Details |
A | HIS567 | |
Chain | Residue | Details |
A | CSD340 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dtw |
Chain | Residue | Details |
A | HIS643 | |