Structure of PDB 1upa Chain C Binding Site BS03

Receptor Information
>1upa Chain C (length=547) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PTAAHALLSRLRDHGVGKVFGVVGREAASILFDEVEGIDFVLTRHEFTAG
VAADVLARITGRPQACWATLGPGMTNLSTGIATSVLDRSPVIALAAQSES
HDIFPNDTHQCLDSVAIVAPMSKYAVELQRPHEITDLVDSAVNAAMTEPV
GPSFISLPVDLLGSSEGIDPPANTPAKPVGVVADGWQKAADQAAALLAEA
KHPVLVVGAAAIRSGAVPAIRALAERLNIPVITTYIAKGVLPVGHELNYG
AVTGYMDGILNFPALQTMFAPVDLVLTVGYDYAEDLRPSMWQKGIEKKTV
RISPTVNPIPRVYRPDVDVVTDVLAFVEHFETATASFGAKQRHDIEPLRA
RIAEFLADPETYEDGMRVHQVIDSMNTVMEEAAEPGEGTIVSDIGFFRHY
GVLFARADQPFGFLTSAGCSSFGYGIPAAIGAQMARPDQPTFLIAGDGGF
HSNSSDLETIARLNLPIVTVVVNNDTNGLIELYQNIGHHRSHDPAVKFGG
VDFVALAEANGVDATRATNREELLAALRKGAELGRPFLIEVPVNYDF
Ligand information
Ligand IDSO4
InChIInChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKeyQAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[O-]S(=O)(=O)[O-]
CACTVS 3.341[O-][S]([O-])(=O)=O
ACDLabs 10.04[O-]S([O-])(=O)=O
FormulaO4 S
NameSULFATE ION
ChEMBL
DrugBankDB14546
ZINC
PDB chain1upa Chain C Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1upa Crystal Structure and Mechanistic Implications of N2-(2-Carboxyethyl)Arginine Synthase, the First Enzyme in the Clavulanic Acid Biosynthesis Pathway
Resolution2.35 Å
Binding residue
(original residue number in PDB)		Y271 R414 H415
Binding residue
(residue number reindexed from 1)		Y255 R398 H399
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 I259 L286 I394 S420 F422 D447 N474 T476 N477 L479 I480 Y483 Y545
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:1upa, PDBe:1upa, PDBj:1upa
PDBsum1upa
PubMed14623876
UniProtQ9LCV9|CEAS_STRCL N(2)-(2-carboxyethyl)arginine synthase (Gene Name=ceaS)

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