Structure of PDB 1on3 Chain F

Receptor sequence

>1on3F (length=517) Species: 1744 (Propionibacterium freudenreichii)

KLASTMEGRVEQLAEQRQVIEAGGGERRVEKQHSQGKQTARERLNNLLDP
HSFDEVGAFRKHRTTLFGMDKAVVPADGVVTGRGTILGRPVHAASQDFTV
MGGSAGETQSTKVVETMEQALLTGTPFLFFYDSGGARIQEGIDSLSGYGK
MFFANVKLSGVVPQIAIIAGPCAGGASYSPALTDFIIMTKKAHMFITGPQ
VIKSVTGEDVTADELGGAEAHMAISGNIHFVAEDDDAAELIAKKLLSFLP
QNNTEEASFVNPNNDVSPNTELRDIVPIDGKKGYDVRDVIAKIVDWGDYL
EVKAGYATNLVTAFARVNGRSVGIVANQPSVMSGCLDINASDKAAEFVNF
CDSFNIPLVQLVDVPGFLPGVQQEYGGIIRHGAKMLYAYSEATVPKITVV
LRKAYGGSYLAMCNRDLGADAVYAWPSAEIAVMGAEGAANVIFRKEIKAA
DDPDAMRAEKIEEYQNAFNTPYVAAARGQVDDVIDPADTRRKIASALEMY
ATKRQTRPAKKHGNFPC

3D structure

• PDB: 1on3 Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core
• Chain: F
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A143 G181 G182 F374 G414 S415
• Catalytic site (residue number reindexed from 1): A136 G174 G175 F367 G407 S408
• Enzyme Commision number: 2.1.3.1: methylmalonyl-CoA carboxytransferase.

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	MCA	F	G413 V439 M440 R451	G406 V432 M433 R444
BS02	MCA	F	R35 F105 G109 S111 G141 A143 I145 G181 G182	R28 F98 G102 S104 G134 A136 I138 G174 G175
BS03	DXX	F	T204 G205	T197 G198

Gene Ontology

Molecular Function

• GO:0003989 acetyl-CoA carboxylase activity
• GO:0004658 propionyl-CoA carboxylase activity
• GO:0016740 transferase activity
• GO:0016874 ligase activity
• GO:0047154 methylmalonyl-CoA carboxytransferase activity

Biological Process

• GO:0006633 fatty acid biosynthetic process

Cellular Component

• GO:0009317 acetyl-CoA carboxylase complex

External links

• PDB: RCSB:1on3, PDBe:1on3, PDBj:1on3
• PDBsum: 1on3
• PubMed: 12743028
• UniProt: Q8GBW6|12S_PROFR Methylmalonyl-CoA carboxyltransferase 12S subunit