Structure of PDB 8fsi Chain A Binding Site BS02

Receptor Information
>8fsi Chain A (length=245) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEV
TVKDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRECKKEGIH
TCLDTNGFVRHYDPVIDELLEVTDLVMLDLKQMNDEIHKNLVGVSNHRTL
RFAQYLAEKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLP
YHELGKHKWVAMGEEYKLDGVEPPRAETMRRVKGILEQYGHKVMF
Ligand information
Ligand IDSAM
InChIInChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/t7-,8+,10+,11+,14+,27-/m0/s1
InChIKeyMEFKEPWMEQBLKI-FCKMPRQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[S@@+](CC[C@H](N)C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S+](CCC(C(=O)[O-])N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341C[S+](CC[CH](N)C([O-])=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S@@+](CC[C@@H](C(=O)[O-])N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
ACDLabs 10.04[O-]C(=O)C(N)CC[S+](C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H22 N6 O5 S
NameS-ADENOSYLMETHIONINE
ChEMBLCHEMBL1235831
DrugBank
ZINC
PDB chain8fsi Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8fsi Computational engineering of previously crystallized pyruvate formate-lyase activating enzyme reveals insights into SAM binding and reductive cleavage.
Resolution1.46 Å
Binding residue
(original residue number in PDB)		Y35 H37 G77 G78 E79 D104 T105 D129 K131 V168 H202
Binding residue
(residue number reindexed from 1)		Y35 H37 G77 G78 E79 D104 T105 D129 K131 V168 H202
Annotation score5
Enzymatic activity
Enzyme Commision number 1.97.1.4: [formate-C-acetyltransferase]-activating enzyme.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0030955 potassium ion binding
GO:0043365 [formate-C-acetyltransferase]-activating enzyme activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006974 DNA damage response
GO:0051604 protein maturation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8fsi, PDBe:8fsi, PDBj:8fsi
PDBsum8fsi
PubMed37156396
UniProtP0A9N4|PFLA_ECOLI Pyruvate formate-lyase 1-activating enzyme (Gene Name=pflA)

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