Structure of PDB 3ib9 Chain B

Receptor sequence
>3ib9B (length=521) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
DIHTTAGKLADLRRRIEEATHAGSARAVEKQHAKGKLTARERIDLLLDEG
SFVELDEFARHRSTNFGLDANRPYGDGVVTGYGTVDGRPVAVFSQDFTVF
GGALGEVYGQKIVKVMDFALKTGCPVVGINDSGGARIQEGVASLGAYGEI
FRRNTHASGVIPQISLVVGPCAGGAVYSPAITDFTVMVDQTSHMFITGPD
VIKTVTGEDVGFEELGGARTHNSTSGVAHHMAGDEKDAVEYVKQLLSYLP
SNNLSEPPAFPEEADLAVTDEDAELDTIVPDSANQPYDMHSVIEHVLDDA
EFFETQPLFAPNILTGFGRVEGRPVGIVANQPMQFAGCLDITASEKAARF
VRTCDAFNVPVLTFVDVPGFLPGVDQEHDGIIRRGAKLIFAYAEATVPLI
TVITRKAFGGAYLVMGSKHLGADLNLAWPTAQIAVMGAQGAVNILHRRTI
ADAGDDAEATRARLIQEYEDALLNPYTAAERGYVDAVIMPSDTRRHIVRG
LRQLRTKRESLPPKKHGNIPL
3D structure
PDB3ib9 Crystal structures and mutational analyses of acyl-CoA carboxylase beta subunit of Streptomyces coelicolor.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A144 G182 G183 F379 G419 A420
Catalytic site (residue number reindexed from 1) A135 G173 G174 F370 G410 A411
Enzyme Commision number ?
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 BTN B P179 H202 F221 P170 H193 F212
Gene Ontology
Molecular Function
GO:0003989 acetyl-CoA carboxylase activity
GO:0004658 propionyl-CoA carboxylase activity
GO:0016874 ligase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
Cellular Component
GO:0009317 acetyl-CoA carboxylase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ib9, PDBe:3ib9, PDBj:3ib9
PDBsum3ib9
PubMed20690600
UniProtQ9X4K7

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