Structure of PDB 1oqb Chain D

Receptor sequence
>1oqbD (length=346) Species: 3988 (Ricinus communis) [Search protein sequence]
FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPVEKCWQPQDF
LPDPASDGFDEQVRELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLNT
LDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEK
TIQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADMMRKKISMPA
HLMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEFLVGRWKVDKLTGLS
AEGQKAQDYVCRLPPRIRRLEERAQGRAKEAPTMPFSWIFDRQVKL
3D structure
PDB1oqb Azide and Acetate Complexes plus two iron-depleted Crystal Structures of the Di-iron Enzyme delta9 Stearoyl-ACP Desaturase-Implications for Oxygen Activation and Catalytic Intermediates
ChainD
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 FE2 D E105 E143 H146 E229 E88 E126 H129 E212
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:1oqb, PDBe:1oqb, PDBj:1oqb
PDBsum1oqb
PubMed12704186
UniProtP22337|STAD_RICCO Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic

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