1OZG
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 |
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 | HE3700 |
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 | HOH752 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 704 |
Chain | Residue |
B | ASP447 |
B | ASP474 |
B | GLY476 |
B | HE3705 |
B | HOH706 |
site_id | AC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE HE3 A 700 |
Chain | Residue |
A | ILE32 |
A | PRO33 |
A | GLU57 |
A | PRO83 |
A | ASN87 |
A | MET394 |
A | GLY395 |
A | SER396 |
A | PHE397 |
A | GLN420 |
A | MET422 |
A | ASP447 |
A | GLY448 |
A | GLY449 |
A | ASP474 |
A | GLY476 |
A | TYR477 |
A | ASN478 |
A | MET479 |
A | VAL480 |
A | TYR543 |
A | MG699 |
A | HOH740 |
A | HOH763 |
A | HOH776 |
A | HOH959 |
site_id | AC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE HE3 B 705 |
Chain | Residue |
B | ILE32 |
B | PRO33 |
B | GLU57 |
B | THR80 |
B | PRO83 |
B | ASN87 |
B | MET394 |
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 | HOH759 |
B | HOH769 |
B | HOH934 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG A 691 |
Chain | Residue |
A | SER254 |
A | GLN353 |
A | ARG356 |
A | PEG692 |
A | HOH896 |
B | ARG375 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG A 692 |
Chain | Residue |
A | ARG356 |
A | GLU357 |
A | ARG362 |
A | PEG691 |
A | HOH997 |
B | ARG378 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 693 |
Chain | Residue |
A | PRO498 |
A | GLU506 |
A | GLY509 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 694 |
Chain | Residue |
A | HOH963 |
B | ALA520 |
B | THR524 |
A | ARG228 |
A | HOH897 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 695 |
Chain | Residue |
A | ARG228 |
A | ALA247 |
A | HOH963 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG B 701 |
Chain | Residue |
B | PRO498 |
B | GLY509 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG B 702 |
Chain | Residue |
B | LEU262 |
B | ASN417 |
B | GLN420 |
B | MET479 |
B | HOH761 |
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 |