1OZF
The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 697 |
| Chain | Residue |
| A | PHE256 |
| A | HOH756 |
| 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 699 |
| Chain | Residue |
| A | ASP447 |
| A | ASP474 |
| A | GLY476 |
| A | TPP700 |
| A | HOH740 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 703 |
| Chain | Residue |
| B | ARG259 |
| B | GLN266 |
| B | ARG352 |
| B | ALA402 |
| B | ARG403 |
| B | LEU405 |
| B | TYR406 |
| B | HOH753 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 704 |
| Chain | Residue |
| B | ASP447 |
| B | ASP474 |
| B | GLY476 |
| B | TPP705 |
| B | HOH706 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP A 700 |
| Chain | Residue |
| A | PRO33 |
| A | GLU57 |
| A | ASN87 |
| 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 | MG699 |
| A | HOH740 |
| A | HOH763 |
| A | HOH966 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP B 705 |
| Chain | Residue |
| B | ILE32 |
| B | PRO33 |
| B | GLU57 |
| B | ASN87 |
| B | GLY395 |
| B | SER396 |
| 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 | TYR543 |
| B | MG704 |
| B | HOH706 |
| B | HOH760 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 690 |
| Chain | Residue |
| A | ASP198 |
| A | LYS202 |
| A | ALA205 |
| A | ASN334 |
| A | ASP336 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 691 |
| Chain | Residue |
| A | ARG356 |
| A | PEG692 |
| A | HOH896 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG A 692 |
| Chain | Residue |
| A | GLN353 |
| A | ARG356 |
| A | GLU357 |
| A | ASP360 |
| A | PEG691 |
| B | ARG375 |
| B | ARG378 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 693 |
| Chain | Residue |
| A | PRO498 |
| A | GLU506 |
| A | PHE508 |
| A | GLY509 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 694 |
| Chain | Residue |
| B | ALA520 |
| B | THR524 |
| A | HIS235 |
| A | PEG695 |
| A | HOH897 |
| A | HOH971 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 695 |
| Chain | Residue |
| A | ARG228 |
| A | GLU232 |
| A | ALA247 |
| A | ASN252 |
| A | PEG694 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 696 |
| Chain | Residue |
| A | ILE399 |
| A | GLN483 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG B 701 |
| Chain | Residue |
| B | PRO498 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 702 |
| Chain | Residue |
| B | LEU262 |
| B | GLN420 |
| B | HOH762 |
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 | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG159 | |
| A | PHE263 | |
| A | ASP304 | |
| A | ASP447 | |
| B | ARG159 | |
| B | PHE263 | |
| B | ASP304 | |
| B | ASP447 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | PRO547 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | PRO547 |
| 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 |
