Structure of PDB 1upc Chain A Binding Site BS01

Receptor Information
>1upc Chain A (length=559) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PTAAHALLSRLRDHGVGKVFGVVGREAASILFDEVEGIDFVLTRHEFTAG
VAADVLARITGRPQACWATLGPGMTNLSTGIATSVLDRSPVIALAAQSES
HDIFPNDTHQCLDSVAIVAPMSKYAVELQRPHEITDLVDSAVNAAMTEPV
GPSFISLPVDLLGSSEGIDTPNPPANTPAKPVGVVADGWQKAADQAAALL
AEAKHPVLVVGAAAIRSGAVPAIRALAERLNIPVITTYIAKGVLPVGHEL
NYGAVTGYMDGILNFPALQTMFAPVDLVLTVGYDYAEDLRPSMWQKGIEK
KTVRISPTVNPIPRVYRPDVDVVTDVLAFVEHFETATASFGAKQRHDIEP
LRARIAEFLADPETYEDGMRVHQVIDSMNTVMEEAAEPGEGTIVSDIGFF
RHYGVLFARADQPFGFLTSAGCSSFGYGIPAAIGAQMARPDQPTFLIAGD
GGFHSNSSDLETIARLNLPIVTVVVNNDTNGLIELYQNIGHHRSHDPAVK
FGGVDFVALAEANGVDATRATNREELLAALRKGAELGRPFLIEVPVNYDF
QPGGFGALS
Ligand information
Ligand IDTPP
InChIInChI=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
InChIKeyAYEKOFBPNLCAJY-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N
FormulaC12 H19 N4 O7 P2 S
NameTHIAMINE DIPHOSPHATE
ChEMBLCHEMBL1236376
DrugBank
ZINCZINC000008215517
PDB chain1upc Chain A Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1upc Crystal Structure and Mechanistic Implications of N2-(2-Carboxyethyl)Arginine Synthase, the First Enzyme in the Clavulanic Acid Biosynthesis Pathway
Resolution2.45 Å
Binding residue
(original residue number in PDB)		I410 G411 F412 F413 F438 G462 D463 G464 G465 T492 N493 G494 L495 Y561
Binding residue
(residue number reindexed from 1)		I397 G398 F399 F400 F425 G449 D450 G451 G452 T479 N480 G481 L482 Y548
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) V33 G35 R36 E37 A38 E57 T80 H120 Q121 C122 V170 I275 L302 I410 S436 F438 D463 N490 T492 N493 L495 I496 Y499 Y561
Catalytic site (residue number reindexed from 1) V22 G24 R25 E26 A27 E46 T69 H109 Q110 C111 V159 I262 L289 I397 S423 F425 D450 N477 T479 N480 L482 I483 Y486 Y548
Enzyme Commision number 2.5.1.66: N(2)-(2-carboxyethyl)arginine synthase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003984 acetolactate synthase activity
GO:0016740 transferase activity
GO:0030976 thiamine pyrophosphate binding
GO:0033848 N2-(2-carboxyethyl)arginine synthase activity
GO:0046872 metal ion binding
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0009097 isoleucine biosynthetic process
GO:0009099 L-valine biosynthetic process
Cellular Component
GO:0005948 acetolactate synthase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1upc, PDBe:1upc, PDBj:1upc
PDBsum1upc
PubMed14623876
UniProtQ9LCV9|CEAS_STRCL N(2)-(2-carboxyethyl)arginine synthase (Gene Name=ceaS)

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