Structure of PDB 3u0f Chain A Binding Site BS02

Receptor Information

>3u0f Chain A (length=407) Species: 359391 (Brucella abortus 2308)

MRRVVVTGMGIVSSIGSNTEEVTASLREAKSGISRAEEYAELGFRCQVHG
APDIDIESLVDRRAMRFHGRGTAWNHIAMDQAIADAGLTEEEVSNERTGI
IMGSGGPSTRTIVDSADITREKGPKRVGPFAVPKAMSSTASATLATFFKI
KGINYSISSACATSNHCIGNAYEMIQYGKQDRMFAGGCEDLDWTLSVLFD
AMGAMSSKYNDTPSTASRAYDKNRDGFVIAGGAGVLVLEDLETALARGAK
IYGEIVGYGATSDGYDMVAPSGEGAIRCMKMALSTVTSKIDYINPHATST
PAGDAPEIEAIRQIFGAGDVCPPIAATKSLTGHSLGATGVQEAIYSLLMM
QNNFICESAHIEELDPAFADMPIVRKRIDNVQLNTVLSNSFGFGGTNATL
VFQRYQG

Ligand information

• Ligand ID: MOH
• InChI: InChI=1S/CH4O/c1-2/h2H,1H3
• InChIKey: OKKJLVBELUTLKV-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.352
  OpenEye OEToolkits 1.7.0: CO
  ACDLabs 11.02: OC
• Formula: C H4 O
• Name: METHANOL
• ChEMBL: CHEMBL14688
• PDB chain: 3u0f Chain A Residue 412

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3u0f Structural characterization of beta-ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites.
• Resolution: 1.25 Å
• Binding residue (original residue number in PDB): Y39 H49 L191 D192
• Binding residue (residue number reindexed from 1): Y39 H49 L191 D192
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): C161 H296 E307 K328 H333 F391 F393
• Catalytic site (residue number reindexed from 1): C161 H296 E307 K328 H333 F391 F393
• Enzyme Commision number: 2.3.1.41: beta-ketoacyl-[acyl-carrier-protein] synthase I.

Gene Ontology

Molecular Function

• GO:0004315 3-oxoacyl-[acyl-carrier-protein] synthase activity
• GO:0016746 acyltransferase activity
• GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups

Biological Process

• GO:0006633 fatty acid biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:3u0f, PDBe:3u0f, PDBj:3u0f
• PDBsum: 3u0f
• PubMed: 31237717
• UniProt: Q2YQQ9