Structure of PDB 1afr Chain D

Receptor sequence
>1afrD (length=345) Species: 3988 (Ricinus communis) [Search protein sequence]
MPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPVEKCWQPQDFL
PDPASDGFDEQVRELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLNTL
DGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKT
IQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIKL
AQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADMMRKKISMPAH
LMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEFLVGRWKVDKLTGLSA
EGQKAQDYVCRLPPRIRRLEERAQGRAKEAPTMPFSWIFDRQVKL
3D structure
PDB1afr Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins.
ChainD
Resolution2.4 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) W44 E87 E125 H128 E178 T181 D210 E211 H214
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 E143 E196 E229 H232 E125 E178 E211 H214
BS02 FE2 D E105 E143 H146 E229 E87 E125 H128 E211
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0045300 stearoyl-[ACP] desaturase activity
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1afr, PDBe:1afr, PDBj:1afr
PDBsum1afr
PubMed8861937
UniProtP22337|STAD_RICCO Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic

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