Structure of PDB 1oq4 Chain B Binding Site BS02

Receptor Information
>1oq4 Chain B (length=346) Species: 3988 (Ricinus communis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPVEKCWQPQDF
LPDPASDGFDEQVRELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLNT
LDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEK
TIQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADMMRKKISMPA
HLMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEFLVGRWKVDKLTGLS
AEGQKAQDYVCRLPPRIRRLEERAQGRAKEAPTMPFSWIFDRQVKL
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain1oq4 Chain B Residue 365 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1oq4 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.
Resolution2.4 Å
Binding residue
(original residue number in PDB)
E143 E196 E229 H232
Binding residue
(residue number reindexed from 1)
E126 E179 E212 H215
Annotation score1
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.
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1oq4, PDBe:1oq4, PDBj:1oq4
PDBsum1oq4
PubMed12704186
UniProtP22337|STAD_RICCO Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic

[Back to BioLiP]