1OZH
The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.
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 | 0005948 | cellular_component | acetolactate synthase complex |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0034077 | biological_process | butanediol metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003984 | molecular_function | acetolactate synthase activity |
| B | 0005948 | cellular_component | acetolactate synthase complex |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0034077 | biological_process | butanediol metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003984 | molecular_function | acetolactate synthase activity |
| C | 0005948 | cellular_component | acetolactate synthase complex |
| C | 0009097 | biological_process | isoleucine biosynthetic process |
| C | 0009099 | biological_process | L-valine biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0034077 | biological_process | butanediol metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003984 | molecular_function | acetolactate synthase activity |
| D | 0005948 | cellular_component | acetolactate synthase complex |
| D | 0009097 | biological_process | isoleucine biosynthetic process |
| D | 0009099 | biological_process | L-valine biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0034077 | biological_process | butanediol metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1404 |
| Chain | Residue |
| A | PHE256 |
| A | HOH1472 |
| A | GLY258 |
| A | ARG259 |
| A | GLN266 |
| A | ARG352 |
| A | ALA402 |
| A | ARG403 |
| A | LEU405 |
| A | TYR406 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1405 |
| Chain | Residue |
| A | ASP447 |
| A | ASP474 |
| A | GLY476 |
| A | HE31406 |
| A | HOH1435 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1411 |
| Chain | Residue |
| B | GLY258 |
| B | ARG259 |
| B | GLN266 |
| B | ARG352 |
| B | ALA402 |
| B | TYR406 |
| B | HOH1490 |
| B | HOH1593 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1412 |
| Chain | Residue |
| B | ASP447 |
| B | ASP474 |
| B | GLY476 |
| B | HE31413 |
| B | HOH1453 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 C 1421 |
| Chain | Residue |
| C | GLY258 |
| C | ARG259 |
| C | GLN266 |
| C | ARG352 |
| C | ALA402 |
| C | TYR406 |
| C | HOH1487 |
| C | HOH1594 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 1422 |
| Chain | Residue |
| C | ASP447 |
| C | ASP474 |
| C | GLY476 |
| C | HE31423 |
| C | HOH1451 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 D 1431 |
| Chain | Residue |
| D | PHE256 |
| D | GLY258 |
| D | ARG259 |
| D | GLN266 |
| D | ARG352 |
| D | ARG403 |
| D | TYR406 |
| D | HOH1509 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1432 |
| Chain | Residue |
| D | ASP447 |
| D | ASP474 |
| D | GLY476 |
| D | HE31433 |
| D | HOH1473 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PGE A 1402 |
| Chain | Residue |
| A | HIS235 |
| A | SER254 |
| A | PGE1403 |
| A | HOH1573 |
| A | HOH1590 |
| A | HOH1714 |
| C | ALA520 |
| C | THR524 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE A 1403 |
| Chain | Residue |
| A | ALA247 |
| A | ASN252 |
| A | PGE1402 |
| A | HOH1543 |
| A | HOH1723 |
| site_id | BC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HE3 A 1406 |
| Chain | Residue |
| A | MET394 |
| A | GLY395 |
| A | SER396 |
| A | PHE397 |
| A | GLN420 |
| A | MET422 |
| A | GLY446 |
| A | ASP447 |
| A | GLY448 |
| A | GLY449 |
| A | GLN452 |
| A | ASP474 |
| A | GLY476 |
| A | TYR477 |
| A | ASN478 |
| A | MET479 |
| A | VAL480 |
| A | TYR543 |
| A | MG1405 |
| A | HOH1428 |
| A | HOH1432 |
| A | HOH1435 |
| A | HOH1483 |
| B | PRO33 |
| B | GLU57 |
| B | ASN87 |
| site_id | BC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HE3 B 1413 |
| Chain | Residue |
| B | PHE397 |
| B | GLN420 |
| B | MET422 |
| B | GLY446 |
| B | ASP447 |
| B | GLY448 |
| B | GLY449 |
| B | GLN452 |
| B | ASP474 |
| B | GLY476 |
| B | TYR477 |
| B | ASN478 |
| B | MET479 |
| B | VAL480 |
| B | TYR543 |
| B | MG1412 |
| B | HOH1417 |
| B | HOH1446 |
| B | HOH1450 |
| B | HOH1453 |
| A | PRO33 |
| A | GLU57 |
| A | ASN87 |
| B | MET394 |
| B | GLY395 |
| B | SER396 |
| site_id | BC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE HE3 C 1423 |
| Chain | Residue |
| C | MET394 |
| C | GLY395 |
| C | SER396 |
| C | PHE397 |
| C | GLN420 |
| C | MET422 |
| C | GLY446 |
| C | ASP447 |
| C | GLY448 |
| C | GLY449 |
| C | GLN452 |
| C | ASP474 |
| C | GLY476 |
| C | TYR477 |
| C | ASN478 |
| C | MET479 |
| C | VAL480 |
| C | TYR543 |
| C | MG1422 |
| C | HOH1444 |
| C | HOH1448 |
| C | HOH1451 |
| C | HOH1500 |
| D | PRO33 |
| D | GLU57 |
| D | PRO83 |
| D | ASN87 |
| site_id | BC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE HE3 D 1433 |
| Chain | Residue |
| C | ILE32 |
| C | PRO33 |
| C | GLU57 |
| C | PRO83 |
| C | ASN87 |
| D | MET394 |
| D | GLY395 |
| D | SER396 |
| D | PHE397 |
| D | GLN420 |
| D | MET422 |
| D | GLY446 |
| D | ASP447 |
| D | GLY448 |
| D | GLY449 |
| D | GLN452 |
| D | ASP474 |
| D | GLY476 |
| D | TYR477 |
| D | ASN478 |
| D | MET479 |
| D | VAL480 |
| D | TYR543 |
| D | MG1432 |
| D | HOH1437 |
| D | HOH1466 |
| D | HOH1470 |
| D | HOH1473 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 1400 |
| Chain | Residue |
| A | GLU506 |
| A | GLY509 |
| B | PRO498 |
| B | HOH1746 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 1401 |
| Chain | Residue |
| A | SER254 |
| A | GLN353 |
| A | ARG356 |
| A | HOH1697 |
| C | ARG375 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 1410 |
| Chain | Residue |
| A | PRO498 |
| B | GLU506 |
| B | GLY509 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG C 1420 |
| Chain | Residue |
| C | GLU506 |
| C | SER507 |
| C | GLY509 |
| D | PRO498 |
| D | ASP500 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG D 1430 |
| Chain | Residue |
| C | PRO498 |
| D | GLU506 |
| D | SER507 |
| D | PHE508 |
| D | GLY509 |
| D | HOH1699 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGawlvnPerkvVsVsGDGG |
| Chain | Residue | Details |
| A | ILE430-GLY449 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG159 | |
| C | PHE263 | |
| C | ASP304 | |
| C | ASP447 | |
| D | ARG159 | |
| D | PHE263 | |
| D | ASP304 | |
| D | ASP447 | |
| A | PHE263 | |
| A | ASP304 | |
| A | ASP447 | |
| B | ARG159 | |
| B | PHE263 | |
| B | ASP304 | |
| B | ASP447 | |
| C | ARG159 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| A | MET422 | |
| A | MET394 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| B | MET422 | |
| B | MET394 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| C | MET422 | |
| C | MET394 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| D | MET422 | |
| D | MET394 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 722 |
| Chain | Residue | Details |
| A | MET394 | electrostatic stabiliser |
| A | MET422 | steric role |
| A | ASP447 | metal ligand |
| A | ASP474 | metal ligand |
| A | GLY476 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 722 |
| Chain | Residue | Details |
| B | MET394 | electrostatic stabiliser |
| B | MET422 | steric role |
| B | ASP447 | metal ligand |
| B | ASP474 | metal ligand |
| B | GLY476 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 722 |
| Chain | Residue | Details |
| C | MET394 | electrostatic stabiliser |
| C | MET422 | steric role |
| C | ASP447 | metal ligand |
| C | ASP474 | metal ligand |
| C | GLY476 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 722 |
| Chain | Residue | Details |
| D | MET394 | electrostatic stabiliser |
| D | MET422 | steric role |
| D | ASP447 | metal ligand |
| D | ASP474 | metal ligand |
| D | GLY476 | metal ligand |
