1T9D
Crystal Structure Of Yeast Acetohydroxyacid Synthase In Complex With A Sulfonylurea Herbicide, Metsulfuron 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 | 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 |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0003984 | molecular_function | acetolactate synthase activity |
C | 0005739 | cellular_component | mitochondrion |
C | 0005948 | cellular_component | acetolactate synthase complex |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
C | 0009097 | biological_process | isoleucine biosynthetic process |
C | 0009099 | biological_process | valine biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0030976 | molecular_function | thiamine pyrophosphate binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0003984 | molecular_function | acetolactate synthase activity |
D | 0005739 | cellular_component | mitochondrion |
D | 0005948 | cellular_component | acetolactate synthase complex |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
D | 0009097 | biological_process | isoleucine biosynthetic process |
D | 0009099 | biological_process | valine biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0030976 | molecular_function | thiamine pyrophosphate binding |
D | 0046872 | molecular_function | metal ion binding |
D | 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 | HOH4274 |
B | HOH5858 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 699 |
Chain | Residue |
B | P25698 |
B | HOH4287 |
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 | HOH4043 |
A | HOH5543 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1699 |
Chain | Residue |
A | ASP550 |
A | ASN577 |
A | GLU579 |
A | P251698 |
A | HOH4061 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K D 2696 |
Chain | Residue |
D | GLN343 |
D | ASP350 |
D | GLN506 |
D | TRP508 |
D | HOH4801 |
D | HOH5353 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 2699 |
Chain | Residue |
D | ASP550 |
D | ASN577 |
D | GLU579 |
D | P222702 |
D | HOH4819 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K C 3696 |
Chain | Residue |
C | GLN343 |
C | ASP350 |
C | GLN506 |
C | TRP508 |
C | HOH5037 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 3699 |
Chain | Residue |
C | ASP550 |
C | ASN577 |
C | GLU579 |
C | P223702 |
C | HOH5774 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 1MM A 695 |
Chain | Residue |
A | MET354 |
A | ASP379 |
A | ARG380 |
A | MET582 |
A | TRP586 |
A | FAD701 |
A | HOH4173 |
B | GLY116 |
B | ALA117 |
B | VAL191 |
B | PRO192 |
B | PHE201 |
B | GLN202 |
B | LYS251 |
B | HOH4143 |
site_id | BC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE P25 B 698 |
Chain | Residue |
B | VAL497 |
B | GLY498 |
B | GLN499 |
B | HIS500 |
B | GLY549 |
B | ASP550 |
B | ALA551 |
B | SER552 |
B | ASN577 |
B | GLU579 |
B | GLN580 |
B | GLY581 |
B | MET582 |
B | MG699 |
B | HOH4287 |
site_id | BC2 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE FAD A 701 |
Chain | Residue |
A | VAL497 |
A | GLN501 |
A | MET502 |
A | GLY520 |
A | GLY521 |
A | 1MM695 |
A | HOH4015 |
A | HOH4016 |
A | HOH4037 |
A | HOH4160 |
A | HOH5915 |
A | HOH6042 |
B | PHE201 |
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 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PYD A 703 |
Chain | Residue |
A | GLY115 |
A | GLU139 |
A | PRO165 |
A | ASN169 |
A | GLN202 |
B | GLY523 |
B | MET525 |
B | MET555 |
B | GLN580 |
site_id | BC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 1MM B 1695 |
Chain | Residue |
A | GLY116 |
A | ALA117 |
A | VAL191 |
A | PRO192 |
A | ALA200 |
A | PHE201 |
A | GLN202 |
A | LYS251 |
B | ASP379 |
B | ARG380 |
B | MET582 |
B | VAL583 |
B | TRP586 |
B | FAD1701 |
B | HOH5600 |
site_id | BC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE P25 A 1698 |
Chain | Residue |
A | VAL497 |
A | GLY498 |
A | GLN499 |
A | HIS500 |
A | MET525 |
A | GLY549 |
A | ASP550 |
A | ALA551 |
A | SER552 |
A | ASN577 |
A | GLU579 |
A | GLN580 |
A | GLY581 |
A | MET582 |
A | MG1699 |
A | HOH4061 |
site_id | BC6 |
Number of Residues | 39 |
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 | GLN336 |
B | LEU352 |
B | MET354 |
B | HIS355 |
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 | GLN501 |
B | MET502 |
B | SER519 |
B | GLY520 |
B | GLY521 |
B | MET582 |
B | 1MM1695 |
B | HOH4248 |
B | HOH4270 |
B | HOH4302 |
B | HOH4615 |
B | HOH5940 |
B | HOH5956 |
site_id | BC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PYD B 1703 |
Chain | Residue |
A | GLY523 |
A | MET525 |
A | MET555 |
B | PRO114 |
B | GLY115 |
B | GLU139 |
B | PRO165 |
B | ASN169 |
B | GLN202 |
site_id | BC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 1MM C 2695 |
Chain | Residue |
C | GLY116 |
C | ALA117 |
C | VAL191 |
C | PRO192 |
C | PHE201 |
C | LYS251 |
C | HOH4890 |
C | HOH4944 |
C | HOH5740 |
D | MET354 |
D | ASP379 |
D | ARG380 |
D | TRP586 |
D | FAD3701 |
site_id | BC9 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD C 2701 |
Chain | Residue |
C | ARG241 |
C | GLY307 |
C | ALA308 |
C | GLY309 |
C | ASN312 |
C | THR334 |
C | LEU335 |
C | LEU352 |
C | GLY353 |
C | MET354 |
C | HIS355 |
C | GLY374 |
C | ALA375 |
C | ARG376 |
C | ASP378 |
C | ARG380 |
C | VAL381 |
C | PHE406 |
C | GLU407 |
C | VAL408 |
C | ASN412 |
C | GLY425 |
C | ASP426 |
C | ALA427 |
C | GLN501 |
C | MET502 |
C | SER519 |
C | GLY520 |
C | GLY521 |
C | 1MM3695 |
C | HOH5008 |
C | HOH5017 |
C | HOH5034 |
C | HOH5067 |
C | HOH5764 |
C | HOH6001 |
D | PHE201 |
site_id | CC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE P22 D 2702 |
Chain | Residue |
D | VAL497 |
D | GLY498 |
D | GLN499 |
D | HIS500 |
D | MET525 |
D | GLY549 |
D | ASP550 |
D | ALA551 |
D | SER552 |
D | ASN577 |
D | GLU579 |
D | GLN580 |
D | GLY581 |
D | MET582 |
D | MG2699 |
D | HOH4819 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PYD C 2703 |
Chain | Residue |
C | PRO114 |
C | GLY115 |
C | GLU139 |
C | PRO165 |
C | ASN169 |
C | GLN202 |
D | GLY523 |
D | MET525 |
site_id | CC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 1MM C 3695 |
Chain | Residue |
C | MET354 |
C | ASP379 |
C | ARG380 |
C | MET582 |
C | VAL583 |
C | TRP586 |
C | FAD2701 |
C | HOH4789 |
C | HOH5408 |
D | GLY116 |
D | ALA117 |
D | VAL191 |
D | PRO192 |
D | PHE201 |
D | GLN202 |
D | LYS251 |
site_id | CC4 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE FAD D 3701 |
Chain | Residue |
C | PHE201 |
C | 1MM2695 |
D | ASP180 |
D | ARG241 |
D | GLY307 |
D | ALA308 |
D | GLY309 |
D | ASN312 |
D | THR334 |
D | LEU335 |
D | GLN336 |
D | LEU352 |
D | GLY353 |
D | MET354 |
D | HIS355 |
D | GLY374 |
D | ALA375 |
D | ARG376 |
D | ASP378 |
D | ARG380 |
D | VAL381 |
D | PHE406 |
D | GLU407 |
D | VAL408 |
D | ASN412 |
D | GLY425 |
D | ASP426 |
D | ALA427 |
D | GLN501 |
D | MET502 |
D | SER519 |
D | GLY520 |
D | GLY521 |
D | HOH4774 |
D | HOH4775 |
D | HOH4795 |
D | HOH4873 |
D | HOH4926 |
D | HOH5146 |
site_id | CC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE P22 C 3702 |
Chain | Residue |
C | VAL497 |
C | GLY498 |
C | GLN499 |
C | HIS500 |
C | MET525 |
C | GLY549 |
C | ASP550 |
C | ALA551 |
C | SER552 |
C | ASN577 |
C | GLU579 |
C | GLN580 |
C | GLY581 |
C | MET582 |
C | MG3699 |
C | HOH5774 |
site_id | CC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PYD D 3703 |
Chain | Residue |
C | VAL497 |
C | GLY523 |
C | MET525 |
D | PRO114 |
D | GLY115 |
D | GLU139 |
D | PRO165 |
D | ASN169 |
D | GLN202 |
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 | 16 |
Details | BINDING: |
Chain | Residue | Details |
C | GLU139 | |
C | ASP550 | |
C | ASN577 | |
C | GLU579 | |
D | GLU139 | |
D | ASP550 | |
D | ASN577 | |
D | GLU579 | |
A | GLU139 | |
A | ASP550 | |
A | ASN577 | |
A | GLU579 | |
B | GLU139 | |
B | ASP550 | |
B | ASN577 | |
B | GLU579 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12496246 |
Chain | Residue | Details |
C | GLU407 | |
D | ARG241 | |
D | HIS355 | |
D | GLU407 | |
A | ARG241 | |
A | HIS355 | |
A | GLU407 | |
B | ARG241 | |
B | HIS355 | |
B | GLU407 | |
C | ARG241 | |
C | HIS355 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 289 |
Chain | Residue | Details |
A | PHE201 | single electron acceptor, single electron donor, single electron relay |
A | LYS251 | steric locator |
A | MET582 | polar interaction, steric role |
A | GLU139 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLN202 | electrostatic stabiliser, hydrogen bond donor |
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 |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 289 |
Chain | Residue | Details |
C | GLU139 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | PHE201 | single electron acceptor, single electron donor, single electron relay |
C | GLN202 | electrostatic stabiliser, hydrogen bond donor |
C | LYS251 | steric locator |
C | MET582 | polar interaction, steric role |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 289 |
Chain | Residue | Details |
D | GLU139 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | PHE201 | single electron acceptor, single electron donor, single electron relay |
D | GLN202 | electrostatic stabiliser, hydrogen bond donor |
D | LYS251 | steric locator |
D | MET582 | polar interaction, steric role |