1N0H
Crystal Structure of Yeast Acetohydroxyacid Synthase in Complex with a Sulfonylurea Herbicide, Chlorimuron Ethyl
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 | 6 |
Details | BINDING SITE FOR RESIDUE K A 696 |
Chain | Residue |
A | GLN343 |
A | ASP350 |
A | GLN506 |
A | TRP508 |
A | HOH753 |
A | HOH1382 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 699 |
Chain | Residue |
A | AYD700 |
A | HOH771 |
A | ASP550 |
A | ASN577 |
A | GLU579 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K B 1696 |
Chain | Residue |
B | GLN343 |
B | ASP350 |
B | GLN506 |
B | TRP508 |
B | HOH1017 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1699 |
Chain | Residue |
B | ASP550 |
B | ASN577 |
B | GLU579 |
B | HOH1032 |
B | TPP1702 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CIE A 695 |
Chain | Residue |
A | MET354 |
A | ASP379 |
A | ARG380 |
A | VAL583 |
A | TRP586 |
A | FAD701 |
B | GLY116 |
B | ALA117 |
B | VAL191 |
B | PRO192 |
B | PHE201 |
B | GLN202 |
B | LYS251 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DTT A 698 |
Chain | Residue |
A | CYS357 |
A | THR359 |
A | LYS455 |
A | TYR458 |
A | TYR460 |
site_id | AC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE AYD 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 | GLU579 |
A | GLN580 |
A | GLY581 |
A | MET582 |
A | VAL583 |
A | MG699 |
A | HOH724 |
A | HOH771 |
A | HOH1108 |
B | PRO114 |
B | GLU139 |
B | PRO165 |
B | ASN169 |
B | GLN202 |
site_id | AC8 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE FAD A 701 |
Chain | Residue |
A | HOH892 |
B | PHE201 |
A | ASP180 |
A | ARG241 |
A | GLY307 |
A | ALA308 |
A | GLY309 |
A | ASN312 |
A | THR334 |
A | LEU335 |
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 | CIE695 |
A | HOH725 |
A | HOH726 |
A | HOH747 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CIE B 1695 |
Chain | Residue |
A | GLY116 |
A | ALA117 |
A | VAL191 |
A | PRO192 |
A | PHE201 |
A | GLN202 |
A | LYS251 |
B | MET354 |
B | ASP379 |
B | ARG380 |
B | MET582 |
B | TRP586 |
B | HOH1520 |
B | FAD1701 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DTT B 1698 |
Chain | Residue |
B | ASP350 |
B | CYS357 |
B | THR359 |
B | LYS455 |
B | TYR458 |
B | PRO459 |
B | HOH1018 |
site_id | BC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE TPP B 1702 |
Chain | Residue |
A | TYR113 |
A | PRO114 |
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 | MET555 |
B | ASN577 |
B | GLU579 |
B | GLN580 |
B | GLY581 |
B | MET582 |
B | VAL583 |
B | HOH1032 |
B | MG1699 |
site_id | BC3 |
Number of Residues | 36 |
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 | ASN412 |
B | GLY425 |
B | ASP426 |
B | ALA427 |
B | GLN501 |
B | MET502 |
B | GLY520 |
B | GLY521 |
B | MET582 |
B | HOH982 |
B | HOH991 |
B | HOH1008 |
B | HOH1013 |
B | HOH1051 |
B | CIE1695 |
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 |