Structure of PDB 1vrg Chain F

Receptor sequence
>1vrgF (length=515) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MSLRDKIEELKKIEKEIEQGGGPEKVEKQHRAGKLTAWERLELLLDPGTF
VEIDKFVEHRNTYFGLDKVKLPRDGVITGVGEINGRKVAVFSQDFTVMGG
SLGEMHAKKIVKLLDLALKMGIPVIGINDSGGARIQEGVDALAGYGEIFL
RNTLASGVVPQITVIAGPCAGGAVYSPALTDFIVMVDQTARMFITGPNVI
KAVTGEEISQEDLGGAMVHNQKSGNAHFLADNDEKAMSLVRTLLSYLPSN
NAEEPPVEDPDTSLETPEDILDILPDNPNKGYDVRDVIKRVVDHGEFFEV
QPYFAKNIVIGFARIQGKTVGIVANQPSVLAGVLDIDSSDKAARFIRFLD
AFNIPILTFVDTPGYLPGVAQEHGGIIRHGAKLLYAYSEATVPKITVILR
KAYGGAYIAMGSKHLGADMVLAWPSAEIAVMGPEGAANIIFKREIEASSN
PEETRRKLIEEYKQQFANPYIAASRGYVDMVIDPRETRKYIMRALEVCET
KVEYRPKKKHGNIPL
3D structure
PDB1vrg Crystal structure of propionyl-CoA carboxylase, beta subunit (TM0716) from THERMOTOGA MARITIMA at 2.30 A resolution
ChainF
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A133 G171 G172 Y365 G405 A406
Catalytic site (residue number reindexed from 1) A133 G171 G172 Y365 G405 A406
Enzyme Commision number 6.4.1.2: acetyl-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 BCT F G196 P197 N198 V199 G196 P197 N198 V199
Gene Ontology
Molecular Function
GO:0004658 propionyl-CoA carboxylase activity
GO:0016874 ligase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:1vrg, PDBe:1vrg, PDBj:1vrg
PDBsum1vrg
PubMed
UniProtQ9WZH5

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