Structure of PDB 5lsq Chain A Binding Site BS01

Receptor Information

>5lsq Chain A (length=342) Species: 317 (Pseudomonas syringae)

NLQTFELPTEVTGCAADISLGRALIQAWQKDGIFQIKTDSEQDRKTQEAM
AASKQFCKEPLTFKSSCVSDLTYSGYVASGEEVTAGKPDFPEIFTVCKDL
SVGDQRVKAGWPCHGPVPWPNNTYQKSMKTFMEELGLAGERLLKLTALGF
ELPINTFTDLTRDGWHHMRVLRFPPQTSTLSRGIGAHTDYGLLVIAAQDD
VGGLYIRPPVEGEKRNRNWLPGESSAGMFEHDEPWTFVTPTPGVWTVFPG
DILQFMTGGQLLSTPHKVKLNTRERFACAYFHEPNFEASAYPLFEPSANE
RIHYGEHFTNMFMRCYPDRITTQRINKENRLAHLEDLKKYSD

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 5lsq Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5lsq Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate.
• Resolution: 1.55 Å
• Binding residue (original residue number in PDB): H189 D191 H268
• Binding residue (residue number reindexed from 1): H187 D189 H266
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 1.13.12.19: 2-oxoglutarate dioxygenase (ethylene-forming).
  1.14.20.7: 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate- forming).

Gene Ontology

Molecular Function

• GO:0016706 2-oxoglutarate-dependent dioxygenase activity
• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity
• GO:0102276 2-oxoglutarate oxygenase/decarboxylase (ethylene-forming) activity

Biological Process

• GO:0009693 ethylene biosynthetic process

External links

• PDB: RCSB:5lsq, PDBe:5lsq, PDBj:5lsq
• PDBsum: 5lsq
• PubMed: 28420789
• UniProt: P32021|EFE_PSESH 2-oxoglutarate-dependent ethylene/succinate-forming enzyme (Gene Name=efe)