Structure of PDB 7orx Chain BBB Binding Site BS02

Receptor Information

>7orx Chain BBB (length=527) Species: 101510 (Rhodococcus jostii RHA1)

ATVSEVTYELLRARGLTTVFGNPGSNELPFLSGMPDDFRYVLGLHEGAVL
SMADGYSLVTGEATLVNLHAASGSGNAMGALTNSVYSHSPLVVTAGQQVR
STIGQEVMLSNVDAGTLMKPLVKWSSEPTCAEDVPRTINQAIHTALLPAK
GPVYVSVPYDDWAAEAPPESAGLLAREVHSAASLSGDQINDLIETLESAT
NPVLVLGPAVDADRANADAVLLAEKLRAPVWIAPSPSRCPFPTRHPSFRG
VLPAGVADLSKTLEGHDLILVVGAPVFRYHQYVPGNYLPGGARLIHVTDD
GGEAARAPIGEAYVAPVGSTLEILANMVKPSDRSPLPPLGDFEEAVSVGA
GLDPAQLFALVRAGAPDDAIYVNESTSTSDAFWSQMDLSHQGSYYFPASG
GLGFGLPAAVGAQLASPDRQVIGLIGDGSANYGITALWSAAQYKIPVVII
ILNNGTYGALRGFSKILNTGETPGLDVPGIDFVHLAEGYGVRGTAVATAE
DFTTAFKSALAADAPTLIEVRTNFDES

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: 7orx Chain BBB Residue 601

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7orx Characterization of Thiamine Diphosphate-Dependent 4-Hydroxybenzoylformate Decarboxylase Enzymes from
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): T377 S378 G401 L403 G427 D428 G429 S430 Y433 T457 Y458 G459 A460
• Binding residue (residue number reindexed from 1): T376 S377 G400 L402 G426 D427 G428 S429 Y432 T456 Y457 G458 A459
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): N23 G25 S26 N27 E28 E47 H70 M109 L110 S111 N112 Y160 P254 H281 S376 G401 L403 D428 N455 T457 Y458 A460 L461 F464
• Catalytic site (residue number reindexed from 1): N22 G24 S25 N26 E27 E46 H69 M108 L109 S110 N111 Y159 P253 H280 S375 G400 L402 D427 N454 T456 Y457 A459 L460 F463
• 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:0016829 lyase activity
• GO:0030976 thiamine pyrophosphate binding
• GO:0050660 flavin adenine dinucleotide binding
• GO:0050695 benzoylformate decarboxylase activity

Biological Process

• GO:0009082 branched-chain amino acid biosynthetic process
• GO:0009097 isoleucine biosynthetic process
• GO:0009099 L-valine biosynthetic process

External links

• PDB: RCSB:7orx, PDBe:7orx, PDBj:7orx
• PDBsum: 7orx
• UniProt: Q0SCE8