Structure of PDB 3e9y Chain A Binding Site BS03

Receptor Information

>3e9y Chain A (length=582) Species: 3702 (Arabidopsis thaliana)

FISRFAPDQPRKGADILVEALERQGVETVFAYPGGASMEIHQALTRSSSI
RNVLPRHEQGGVFAAEGYARSSGKPGICIATSGPGATNLVSGLADALLDS
VPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRIIE
EAFFLATSGRPGPVLVDVPKDIQQQLAIPNWEQAMRLPGYMSRMPKPPED
SHLEQIVRLISESKKPVLYVGGGCLNSSDELGRFVELTGIPVATTLMGLG
SYPCDDELSLHMLGMHGTVYANYAVEHSDLLLAFGVRFDDRVTGKLEAFA
SRAKIVHIDIDSAEIGKNKTPHVSVCGDVKLALQGMNKVLENRAEELKLD
FGVWRNELNVQKQKFPLSFKTFGEAIPPQYAIKVLDELTDGKAIISTGVG
QHQMWAAQFYNYKKPRQWLSSGGLGAMGFGLPAAIGASVANPDAIVVDID
GDGSFIMNVQELATIRVENLPVKVLLLNNQHLGMVMQWEDRFYKANRAHT
FLGDPAQEDEIFPNMLLFAAACGIPAARVTKKADLREAIQTMLDTPGPYL
LDVICPHQEHVLPMIPSGGTFNDVITEGDGRI

Ligand information

• Ligand ID: TDM
• InChI: InChI=1S/C14H22N4O8P2S/c1-8-12(4-5-25-28(23,24)26-27(20,21)22)29-14(9(2)19)18(8)7-11-6-16-10(3)17-13(11)15/h6,19H,4-5,7H2,1-3H3,(H,23,24)(H2,15,16,17)(H2,20,21,22)/b14-9+
• InChIKey: ZZLCKFKIIVXBQU-NTEUORMPSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: Cc1ncc(c(n1)N)CN\2C(=C(S/C2=C(\C)/O)CCO[P@@](=O)(O)OP(=O)(O)O)C
  CACTVS 3.341: C\C(O)=C1/SC(=C(C)N1Cc2cnc(C)nc2N)CCO[P@](O)(=O)O[P](O)(O)=O
  OpenEye OEToolkits 1.5.0: Cc1ncc(c(n1)N)CN2C(=C(SC2=C(C)O)CCOP(=O)(O)OP(=O)(O)O)C
  ACDLabs 10.04: O=P(O)(O)OP(=O)(O)OCCC=1S\C(=C(\O)C)N(C=1C)Cc2cnc(nc2N)C
  CACTVS 3.341: CC(O)=C1SC(=C(C)N1Cc2cnc(C)nc2N)CCO[P](O)(=O)O[P](O)(O)=O
• Formula: C14 H22 N4 O8 P2 S
• Name: 2-[(2E)-3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-2-(1-HYDROXYETHYLIDENE)-4-METHYL-2,3-DIHYDRO-1,3-THIAZOL-5-YL]ETHYL TRIHYDROGEN DIPHOSPHATE;
  2-HYDROXYETHYLTHIAMIN DIPHOSPHATE
• ZINC: ZINC000103557856
• PDB chain: 3e9y Chain A Residue 700

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3e9y Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase.
• Resolution: 3.0 Å
• Binding residue (original residue number in PDB): V485 G486 Q487 H488 M513 G537 G539 S540 N565 H567 L568 G569 M570 V571
• Binding residue (residue number reindexed from 1): V399 G400 Q401 H402 M427 G451 G453 S454 N479 H481 L482 G483 M484 V485
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): Y118 G120 G121 A122 S123 E144 T167 F206 Q207 E208 K256 M351 V378 V485 G511 M513 D538 N565 H567 L568 M570 V571 W574 H643
• Catalytic site (residue number reindexed from 1): Y32 G34 G35 A36 S37 E58 T81 F120 Q121 E122 K170 M265 V292 V399 G425 M427 D452 N479 H481 L482 M484 V485 W488 H557
• Enzyme Commision number: 2.2.1.6: acetolactate synthase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0003984 acetolactate synthase activity
• GO:0030976 thiamine pyrophosphate binding
• GO:0050660 flavin adenine dinucleotide binding

Biological Process

• GO:0009082 branched-chain amino acid biosynthetic process

External links

• PDB: RCSB:3e9y, PDBe:3e9y, PDBj:3e9y
• PDBsum: 3e9y
• PubMed: 19187232
• UniProt: P17597|ILVB_ARATH Acetolactate synthase, chloroplastic (Gene Name=ALS)