Structure of PDB 5ahk Chain B Binding Site BS02

Receptor Information

>5ahk Chain B (length=546) Species: 380021 (Pseudomonas protegens)

MKASDAVAKILADNNVLYGFELIGGMITHLVDSINLLGKTKLVSMHHEQG
AAFAASAVSRVTHHKTLGLALATSGPGATNLITGIADCWLDSHPCIFLTG
QVNTHELKGKRDIRQQGFQELDSVALVTSITKYAYQIKSADELVPCLRKA
IQIAKEGRPGPVLLDIPMDIQRADIDEALLNIAMSDLDFIINKLQNAKKP
LLLIGGGAVNSSGFQKWLEQIELRGIPYVASLKGAEKIKASDLYLGMLGA
YGTRAANHAVQNCDLLLVLGSRMDVRQTGAQPEDFARNAEIIQIDLQEGQ
LNNRVIADFSYQIELSEYFSRFSPLQIPVNNDWSVWTALLKEKFRVTFID
EYTTWNLSPFGLFTQLNKLTERVALDYILDVGNNQMWAAHTLRLNAQQAM
HHSGGLGSMGFAIPAAIGACYAGKKPIIVITGDGGAQLNIQELDIIARDK
LPILTIVMNNHSLGMVRGFSSTYWNGYTSQFKKIGEAYRVESKTIISMQA
FSSALESFLESPRPLLLEVSMSDARECRPRLEYGRAIDQQSPRHDG

Ligand information

• Ligand ID: TPP
• InChI: InChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1
• InChIKey: AYEKOFBPNLCAJY-UHFFFAOYSA-O
• SMILES:
  CACTVS 3.341: Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
  OpenEye OEToolkits 1.5.0: Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
  OpenEye OEToolkits 1.5.0: Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
  CACTVS 3.341: Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
  ACDLabs 10.04: O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N
• Formula: C12 H19 N4 O7 P2 S
• Name: THIAMINE DIPHOSPHATE
• ChEMBL: CHEMBL1236376
• ZINC: ZINC000008215517
• PDB chain: 5ahk Chain B Residue 700

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5ahk The Crystal Structure of the Acetohydroxy Acid Synthase Pf5 from Pseudomonas Protegens
• Resolution: 1.55 Å
• Binding residue (original residue number in PDB): V394 G395 N396 N397 G420 M422 D446 G447 G448 N473 S475 L476 G477 M478
• Binding residue (residue number reindexed from 1): V381 G382 N383 N384 G407 M409 D433 G434 G435 N460 S462 L463 G464 M465
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): L22 G24 G25 M26 I27 E48 T73 K110 R111 F118 Q119 M168 A263 Q290 V394 G420 M422 D446 N473 S475 L476 M478 V479 F482 D545
• Catalytic site (residue number reindexed from 1): L22 G24 G25 M26 I27 E48 T73 K110 R111 F118 Q119 M168 A250 Q277 V381 G407 M409 D433 N460 S462 L463 M465 V466 F469 D523
• Enzyme Commision number: 2.2.1.6: acetolactate synthase.

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0003984 acetolactate synthase activity
• GO:0030976 thiamine pyrophosphate binding
• GO:0046872 metal ion binding
• GO:0050660 flavin adenine dinucleotide binding

Biological Process

• GO:0009097 isoleucine biosynthetic process
• GO:0009099 L-valine biosynthetic process
• GO:0019752 carboxylic acid metabolic process

Cellular Component

• GO:0005948 acetolactate synthase complex

External links

• PDB: RCSB:5ahk, PDBe:5ahk, PDBj:5ahk
• PDBsum: 5ahk
• UniProt: Q4K6F7