Structure of PDB 4pty Chain A Binding Site BS01

Receptor Information

>4pty Chain A (length=174) Species: 83333 (Escherichia coli K-12)

MRVITLAGSPRFPSRSSSLLEYAREKLNGLDVEVYHWNLQNFAPEDLLYA
RFDSPALKTFTEQLQQADGLIVATPVYKAAYSGALKTLLDLLPERALQGK
VVLPLATGGTVAHLLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHR
PQFTPNLQTRLDTALETFWQALHR

Ligand information

• Ligand ID: PO4
• InChI: InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
• InChIKey: NBIIXXVUZAFLBC-UHFFFAOYSA-K
• SMILES:
  CACTVS 3.341: [O-][P]([O-])([O-])=O
  ACDLabs 10.04: [O-]P([O-])([O-])=O
  OpenEye OEToolkits 1.5.0: [O-]P(=O)([O-])[O-]
• Formula: O4 P
• Name: PHOSPHATE ION
• DrugBank: DB14523
• PDB chain: 4pty Chain A Residue 202

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4pty Crystal Structure of Escherichia coli SsuE: Defining a General Catalytic Cycle for FMN Reductases of the Flavodoxin-like Superfamily.
• Resolution: 2.1 Å
• Binding residue (original residue number in PDB): R94 K128
• Binding residue (residue number reindexed from 1): R95 K129
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 1.5.1.38: FMN reductase (NADPH).

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• GO:0008752 FMN reductase (NAD(P)H) activity
• GO:0016491 oxidoreductase activity
• GO:0042803 protein homodimerization activity
• GO:0052873 FMN reductase (NADPH) activity

Biological Process

• GO:0006974 DNA damage response
• GO:0009970 cellular response to sulfate starvation
• GO:0046306 alkanesulfonate catabolic process

Cellular Component

• GO:1990202 FMN reductase complex

External links

• PDB: RCSB:4pty, PDBe:4pty, PDBj:4pty
• PDBsum: 4pty
• PubMed: 24816272
• UniProt: P80644|SSUE_ECOLI FMN reductase (NADPH) (Gene Name=ssuE)