Structure of PDB 1xny Chain B

Receptor sequence

>1xnyB (length=521) Species: 1902 (Streptomyces coelicolor)

DIHTTAGKLADLRRRIEEATHAGSARAVEKQHAKGKLTARERIDLLLDEG
SFVELDEFARHRSTNFGLDANRPYGDGVVTGYGTVDGRPVAVFSQDFTVF
GGALGEVYGQKIVKVMDFALKTGCPVVGINDSGGARIQEGVASLGAYGEI
FRRNTHASGVIPQISLVVGPCAGGAVYSPAITDFTVMVDQTSHMFITGPD
VIKTVTGEDVGFEELGGARTHNSTSGVAHHMAGDEKDAVEYVKQLLSYLP
SNNLSEPPAFPEEADLAVTDEDAELDTIVPDSANQPYDMHSVIEHVLDDA
EFFETQPLFAPNILTGFGRVEGRPVGIVANQPMQFAGCLDITASEKAARF
VRTCDAFNVPVLTFVDVPGFLPGVDQEHDGIIRRGAKLIFAYAEATVPLI
TVITRKAFGGAYDVMGSKHLGADLNLAWPTAQIAVMGAQGAVNILHRRTI
ADAGDDAEATRARLIQEYEDALLNPYTAAERGYVDAVIMPSDTRRHIVRG
LRQLRTKRESLPPKKHGNIPL

3D structure

• PDB: 1xny Crystal Structure of the beta-Subunit of Acyl-CoA Carboxylase: Structure-Based Engineering of Substrate Specificity
• Chain: B
• Resolution: 2.2 Å

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: 6.4.1.3: propionyl-CoA carboxylase.

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	1VU	B	G419 V444 I453 R456 R457	G410 V435 I444 R447 R448
BS02	BTN	B	I205 T206	I196 T197
BS03	1VU	B	F109 A112 G142 G143 A144 R145 I146 Q147 Y156 G182 G183	F100 A103 G133 G134 A135 R136 I137 Q138 Y147 G173 G174
BS04	BTN	B	G378 F379 F417 G418 G419 A420	G369 F370 F408 G409 G410 A411

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

External links

• PDB: RCSB:1xny, PDBe:1xny, PDBj:1xny
• PDBsum: 1xny
• PubMed: 15518551
• UniProt: Q9X4K7