5FEM
Saccharomyces cerevisiae Acetohydroxyacid Synthase in complex with bensulfuron methyl
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 | 0005515 | molecular_function | protein binding |
| 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 | L-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 | 0005515 | molecular_function | protein binding |
| 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 | L-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 | 5 |
| Details | binding site for residue MG A 701 |
| Chain | Residue |
| A | ASP550 |
| A | ASN577 |
| A | GLU579 |
| A | TPP705 |
| A | HOH867 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | binding site for residue FAD A 702 |
| Chain | Residue |
| A | GLY309 |
| A | ASN312 |
| A | THR334 |
| A | LEU335 |
| A | GLN336 |
| A | LEU352 |
| A | GLY353 |
| A | MET354 |
| A | HIS355 |
| 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 | GLN501 |
| A | MET502 |
| A | GLY520 |
| A | GLY521 |
| A | 60G703 |
| A | HOH826 |
| A | HOH855 |
| A | HOH937 |
| A | HOH939 |
| A | HOH1036 |
| B | PHE201 |
| A | ASP180 |
| A | ARG241 |
| A | GLY307 |
| A | ALA308 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue 60G A 703 |
| Chain | Residue |
| A | MET354 |
| A | ASP379 |
| A | ARG380 |
| A | MET582 |
| A | TRP586 |
| A | FAD702 |
| A | HOH864 |
| B | GLY116 |
| B | ALA117 |
| B | VAL191 |
| B | PRO192 |
| B | PHE201 |
| B | GLN202 |
| B | LYS251 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 704 |
| Chain | Residue |
| A | GLN343 |
| A | ASP350 |
| A | GLN506 |
| A | TRP508 |
| A | HOH845 |
| A | HOH1091 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue TPP A 705 |
| Chain | Residue |
| A | VAL497 |
| A | GLY498 |
| A | GLN499 |
| A | HIS500 |
| A | GLY523 |
| A | MET525 |
| A | GLY549 |
| A | ASP550 |
| A | ALA551 |
| A | SER552 |
| A | ASN577 |
| A | GLU579 |
| A | GLN580 |
| A | GLY581 |
| A | MET582 |
| A | VAL583 |
| A | MG701 |
| A | HOH867 |
| B | TYR113 |
| B | PRO114 |
| B | GLY115 |
| B | GLU139 |
| B | PRO165 |
| B | ASN169 |
| B | GLN202 |
| site_id | AC6 |
| Number of Residues | 38 |
| Details | binding site for residue FAD B 701 |
| Chain | Residue |
| B | MET354 |
| B | HIS355 |
| B | GLY374 |
| B | ALA375 |
| B | ARG376 |
| B | ASP378 |
| B | ARG380 |
| B | VAL381 |
| B | GLU407 |
| B | VAL408 |
| B | ASN412 |
| B | GLY425 |
| B | ASP426 |
| B | ALA427 |
| B | GLN501 |
| B | MET502 |
| B | GLY520 |
| B | GLY521 |
| B | 60G703 |
| B | HOH805 |
| B | HOH835 |
| B | HOH845 |
| B | HOH864 |
| B | HOH882 |
| B | HOH953 |
| A | PHE201 |
| B | ASP180 |
| B | ARG241 |
| B | GLY307 |
| B | ALA308 |
| B | GLY309 |
| B | ASN312 |
| B | THR334 |
| B | LEU335 |
| B | GLN336 |
| B | MET351 |
| B | LEU352 |
| B | GLY353 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 702 |
| Chain | Residue |
| B | ASP550 |
| B | ASN577 |
| B | GLU579 |
| B | TPP705 |
| B | HOH873 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue 60G B 703 |
| Chain | Residue |
| A | GLY116 |
| A | VAL191 |
| A | PRO192 |
| A | PHE201 |
| A | GLN202 |
| A | LYS251 |
| B | MET354 |
| B | ARG380 |
| B | MET582 |
| B | TRP586 |
| B | FAD701 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 704 |
| Chain | Residue |
| B | GLN343 |
| B | ASP350 |
| B | GLN506 |
| B | TRP508 |
| B | HOH822 |
| B | HOH1008 |
| site_id | AD1 |
| Number of Residues | 25 |
| Details | binding site for residue TPP B 705 |
| Chain | Residue |
| A | TYR113 |
| A | PRO114 |
| A | GLY115 |
| A | GLU139 |
| A | PRO165 |
| A | ASN169 |
| A | GLN202 |
| B | VAL497 |
| B | GLY498 |
| B | GLN499 |
| B | HIS500 |
| B | GLY523 |
| B | MET525 |
| B | GLY549 |
| B | ASP550 |
| B | ALA551 |
| B | SER552 |
| B | ASN577 |
| B | GLU579 |
| B | GLN580 |
| B | GLY581 |
| B | MET582 |
| B | VAL583 |
| B | MG702 |
| B | HOH873 |
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 | 160 |
| Details | Region: {"description":"Thiamine pyrophosphate binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 82 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12496246","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
