Structure of PDB 2j2f Chain E

Receptor sequence
>2j2fE (length=347) Species: 3988 (Ricinus communis) [Search protein sequence]
PFMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPVEKCWQPQD
FLPDPASDGFDEQVRELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLN
TLDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIE
KTIQYLIGSGMDPRTENSPYLGFIYTSFQERADFISHGNTARQAKEHGDI
KLAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADMMRKKISMP
AHLMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEFLVGRWKVDKLTGL
SAEGQKAQDYVCRLPPRIRRLEERAQGRAKEAPTMPFSWIFDRQVKL
3D structure
PDB2j2f A Single Mutation in the Castor {Delta}9-18:0- Desaturase Changes Reaction Partitioning from Desaturation to Oxidase Chemistry.
ChainE
Resolution2.65 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 D199 D228 E229 H232
Catalytic site (residue number reindexed from 1) W46 E89 E127 H130 E180 D183 D212 E213 H216
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 E E105 E143 H146 E229 E89 E127 H130 E213
BS02 FE E E143 E196 E229 H232 E127 E180 E213 H216
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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Biological Process
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Cellular Component
External links
PDB RCSB:2j2f, PDBe:2j2f, PDBj:2j2f
PDBsum2j2f
PubMed17088542
UniProtP22337|STAD_RICCO Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic

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