1JSC
Crystal Structure of the Catalytic Subunit of Yeast Acetohydroxyacid Synthase: A target for Herbicidal Inhibitors
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 | 0005739 | cellular_component | mitochondrion |
A | 0005948 | cellular_component | acetolactate synthase complex |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
A | 0009097 | biological_process | isoleucine biosynthetic process |
A | 0009099 | biological_process | valine biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
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 | 0005739 | cellular_component | mitochondrion |
B | 0005948 | cellular_component | acetolactate synthase complex |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
B | 0009097 | biological_process | isoleucine biosynthetic process |
B | 0009099 | biological_process | valine biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
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 | 7 |
Details | BINDING SITE FOR RESIDUE K A 696 |
Chain | Residue |
A | GLN343 |
A | ASP350 |
A | GLN506 |
A | TRP508 |
A | HOH772 |
A | HOH1029 |
A | HOH1033 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 699 |
Chain | Residue |
A | TPP700 |
A | HOH795 |
A | HOH796 |
A | ASP550 |
A | ASN577 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K B 1696 |
Chain | Residue |
B | GLN343 |
B | GLN506 |
B | TRP508 |
B | HOH802 |
B | HOH1028 |
B | HOH1034 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1699 |
Chain | Residue |
B | ASP550 |
B | ASN577 |
B | HOH748 |
B | HOH794 |
B | TPP1700 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 2HP A 698 |
Chain | Residue |
A | GLY115 |
A | GLY116 |
A | GLN202 |
A | HOH823 |
B | TPP1700 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 2HP B 1697 |
Chain | Residue |
A | HIS126 |
B | HIS597 |
B | THR598 |
B | HIS599 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 2HP B 1698 |
Chain | Residue |
A | TPP700 |
B | GLY116 |
B | GLN202 |
B | HOH791 |
site_id | AC8 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE TPP A 700 |
Chain | Residue |
A | VAL497 |
A | GLY498 |
A | GLN499 |
A | HIS500 |
A | GLY523 |
A | MET525 |
A | GLY549 |
A | ASP550 |
A | ALA551 |
A | SER552 |
A | MET555 |
A | ASN577 |
A | MG699 |
A | HOH795 |
A | HOH796 |
A | HOH825 |
A | HOH1011 |
B | TYR113 |
B | PRO114 |
B | GLU139 |
B | PRO165 |
B | ASN169 |
B | GLN202 |
B | 2HP1698 |
site_id | AC9 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD A 701 |
Chain | Residue |
A | ARG241 |
A | GLY307 |
A | ALA308 |
A | GLY309 |
A | ASN312 |
A | THR334 |
A | LEU335 |
A | GLN336 |
A | LEU352 |
A | GLY353 |
A | MET354 |
A | HIS355 |
A | GLY356 |
A | GLY374 |
A | ALA375 |
A | ARG376 |
A | ASP378 |
A | ARG380 |
A | VAL381 |
A | GLU407 |
A | VAL408 |
A | ASN412 |
A | GLY425 |
A | ASP426 |
A | ALA427 |
A | HOH797 |
A | HOH798 |
A | HOH908 |
A | HOH963 |
A | HOH1000 |
A | HOH1003 |
B | PHE201 |
site_id | BC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE TPP B 1700 |
Chain | Residue |
B | VAL497 |
B | GLY498 |
B | GLN499 |
B | HIS500 |
B | GLY523 |
B | MET525 |
B | ASP550 |
B | ALA551 |
B | SER552 |
B | MET555 |
B | ASN577 |
B | HOH748 |
B | HOH794 |
B | HOH831 |
B | HOH1027 |
B | MG1699 |
A | TYR113 |
A | PRO114 |
A | GLU139 |
A | PRO165 |
A | ASN169 |
A | GLN202 |
A | 2HP698 |
site_id | BC2 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD B 1701 |
Chain | Residue |
A | PHE201 |
B | ARG241 |
B | GLY307 |
B | ALA308 |
B | GLY309 |
B | ASN312 |
B | THR334 |
B | LEU335 |
B | MET351 |
B | LEU352 |
B | GLY353 |
B | MET354 |
B | HIS355 |
B | GLY356 |
B | GLY374 |
B | ALA375 |
B | ARG376 |
B | ASP378 |
B | ARG380 |
B | VAL381 |
B | PHE406 |
B | GLU407 |
B | VAL408 |
B | ASN412 |
B | GLY425 |
B | ASP426 |
B | ALA427 |
B | MET502 |
B | GLY520 |
B | GLY521 |
B | HOH741 |
B | HOH777 |
B | HOH828 |
B | HOH863 |
Functional Information from PROSITE/UniProt
site_id | PS00187 |
Number of Residues | 20 |
Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaqvakPeslvIdIdGDAS |
Chain | Residue | Details |
A | ILE533-SER552 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU139 | |
A | ASP550 | |
A | ASN577 | |
A | GLU579 | |
B | GLU139 | |
B | ASP550 | |
B | ASN577 | |
B | GLU579 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12496246 |
Chain | Residue | Details |
A | ARG241 | |
A | HIS355 | |
A | GLU407 | |
B | ARG241 | |
B | HIS355 | |
B | GLU407 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 289 |
Chain | Residue | Details |
A | GLU139 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | PHE201 | single electron acceptor, single electron donor, single electron relay |
A | GLN202 | electrostatic stabiliser, hydrogen bond donor |
A | LYS251 | steric locator |
A | MET582 | polar interaction, steric role |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 289 |
Chain | Residue | Details |
B | GLU139 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | PHE201 | single electron acceptor, single electron donor, single electron relay |
B | GLN202 | electrostatic stabiliser, hydrogen bond donor |
B | LYS251 | steric locator |
B | MET582 | polar interaction, steric role |