Structure of PDB 1oq4 Chain F

Receptor sequence

>1oq4F (length=346) Species: 3988 (Ricinus communis)

FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPVEKCWQPQDF
LPDPASDGFDEQVRELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLNT
LDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEK
TIQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADMMRKKISMPA
HLMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEFLVGRWKVDKLTGLS
AEGQKAQDYVCRLPPRIRRLEERAQGRAKEAPTMPFSWIFDRQVKL

3D structure

• PDB: 1oq4 Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta 9 stearoyl-ACP desaturase- implications for oxygen activation and catalytic intermediates.
• Chain: F
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): W62 E105 E143 H146 E196 T199 D228 E229 H232
• Catalytic site (residue number reindexed from 1): W45 E88 E126 H129 E179 T182 D211 E212 H215
• Enzyme Commision number: 1.14.19.2: stearoyl-[acyl-carrier-protein] 9-desaturase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FE	F	E105 E143 H146 E229	E88 E126 H129 E212
BS02	FE	F	E143 E196 E229 H232	E126 E179 E212 H215
BS03	AZI	F	E143 E196	E126 E179

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• GO:0016491 oxidoreductase activity
• GO:0045300 stearoyl-[ACP] desaturase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006631 fatty acid metabolic process
• GO:0006633 fatty acid biosynthetic process

Cellular Component

• GO:0009507 chloroplast

External links

• PDB: RCSB:1oq4, PDBe:1oq4, PDBj:1oq4
• PDBsum: 1oq4
• PubMed: 12704186
• UniProt: P22337|STAD_RICCO Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic