1T9C
Crystal Structure Of Yeast Acetohydroxyacid Synthase In Complex With A Sulfonylurea Herbicide, Sulfometuron 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 | 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 | 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 | 6 |
| Details | BINDING SITE FOR RESIDUE K B 696 |
| Chain | Residue |
| B | GLN343 |
| B | ASP350 |
| B | GLN506 |
| B | TRP508 |
| B | HOH4254 |
| B | HOH4990 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 699 |
| Chain | Residue |
| B | P23700 |
| B | HOH4006 |
| B | ASP550 |
| B | ASN577 |
| B | GLU579 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 1696 |
| Chain | Residue |
| A | GLN343 |
| A | ASP350 |
| A | GLN506 |
| A | TRP508 |
| A | HOH4048 |
| A | HOH4778 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1699 |
| Chain | Residue |
| A | ASP550 |
| A | ASN577 |
| A | GLU579 |
| A | P221702 |
| A | HOH4002 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 1SM A 695 |
| Chain | Residue |
| A | ASP379 |
| A | ARG380 |
| A | MET582 |
| A | TRP586 |
| A | HOH4174 |
| A | HOH4421 |
| B | GLY116 |
| B | ALA117 |
| B | VAL191 |
| B | PRO192 |
| B | PHE201 |
| B | GLN202 |
| B | LYS251 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE P23 B 700 |
| Chain | Residue |
| B | VAL497 |
| B | GLY498 |
| B | GLN499 |
| B | HIS500 |
| B | MET525 |
| B | GLY549 |
| B | ASP550 |
| B | ALA551 |
| B | SER552 |
| B | ASN577 |
| B | GLU579 |
| B | GLN580 |
| B | GLY581 |
| B | MET582 |
| B | MG699 |
| B | HOH4006 |
| site_id | AC7 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD A 701 |
| Chain | Residue |
| A | ASP180 |
| 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 | GLY374 |
| A | ALA375 |
| A | ARG376 |
| A | ASP378 |
| A | ARG380 |
| A | VAL381 |
| A | PHE406 |
| A | GLU407 |
| A | VAL408 |
| A | ASN412 |
| A | GLY425 |
| A | ASP426 |
| A | ALA427 |
| A | GLN501 |
| A | MET502 |
| A | GLY520 |
| A | GLY521 |
| A | MET582 |
| A | HOH4022 |
| A | HOH4023 |
| A | HOH4042 |
| A | HOH4160 |
| A | HOH4342 |
| A | HOH5056 |
| B | PHE201 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 1SM B 1695 |
| Chain | Residue |
| B | MET582 |
| B | TRP586 |
| B | HOH4581 |
| B | HOH4820 |
| A | GLY116 |
| A | ALA117 |
| A | VAL191 |
| A | PRO192 |
| A | PHE201 |
| A | GLN202 |
| A | LYS251 |
| A | HOH4036 |
| B | ASP379 |
| B | ARG380 |
| site_id | AC9 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD B 1701 |
| Chain | Residue |
| A | PHE201 |
| B | ASP180 |
| B | ARG241 |
| B | GLY307 |
| B | ALA308 |
| B | GLY309 |
| B | ASN312 |
| B | THR334 |
| B | LEU335 |
| B | LEU352 |
| B | GLY353 |
| B | MET354 |
| B | HIS355 |
| B | GLY374 |
| B | ALA375 |
| B | ARG376 |
| B | ASP378 |
| B | ARG380 |
| B | VAL381 |
| B | GLU407 |
| B | VAL408 |
| B | SER409 |
| B | ASN412 |
| B | GLY425 |
| B | ASP426 |
| B | ALA427 |
| B | GLN501 |
| B | MET502 |
| B | SER519 |
| B | GLY520 |
| B | GLY521 |
| B | MET582 |
| B | HOH4226 |
| B | HOH4235 |
| B | HOH4248 |
| B | HOH4250 |
| B | HOH4281 |
| B | HOH4447 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE P22 A 1702 |
| Chain | Residue |
| A | VAL497 |
| A | GLY498 |
| A | GLN499 |
| A | HIS500 |
| A | GLY549 |
| A | ASP550 |
| A | ALA551 |
| A | SER552 |
| A | ASN577 |
| A | GLU579 |
| A | GLN580 |
| A | GLY581 |
| A | MET582 |
| A | MG1699 |
| A | HOH4002 |
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 | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | VAL651 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | VAL651 |
| 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 |
