Structure of PDB 3bg5 Chain C

Receptor sequence

>3bg5C (length=1067) Species: 1280 (Staphylococcus aureus)

QIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYL
VGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEG
IKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAE
EAGFPLMIKATSGGGGKGMRIVREESELEDAFHRAKSEAEKSFGNSEVYI
ERYIDNPKHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSP
TLRQRICDAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTIT
EMVTGIDIVKTQILVAAGADLFGEEINMPQQKDITTLGYAIQCRITTEDP
LNDFMPDTGTIIAYRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLSTHA
ISFKQAEEKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEE
TPELFDIQPSLDRGTKTLEYIGNVTINGFPNVEKRPKPDYELASIPTVSS
SKIASFSGTKQLLDEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRV
RTKDMINIASKTADVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRK
AIPNVLFQMLLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNW
VDQMKVANEAVQEAGKISEGTICYTGDILNPERSNIYTLEYYVKLAKELE
REGFHILAIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLT
YKQAIDAGVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGME
SLSHYWSTVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLG
ERFDEVKDMYRRVNFLFGDIVKVTPSSKVVGDMALYMVQNDLDEQSVITD
GYKLDFPESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEP
VDFEKVRELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLD
TPTFFFGMRNGETVEIEIDKGKRLIIKLETISEPDENGNRTIYYAMNGQA
RRIYIKDENTEAMKMET

3D structure

• PDB: 3bg5 Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.
• Chain: C
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K152 K194 S231 H244 R270 T309 E311 E324 N326 R328 E332 R377 D572 D678 K741 H771 H773 I794 S800 M801 T840 T908 S910 V922 N924 Q929
• Catalytic site (residue number reindexed from 1): K117 K159 S196 H209 R235 T274 E276 E288 N290 R292 E296 R344 D540 D646 K710 H739 H741 I762 S768 M769 T808 T874 S876 V888 N890 Q895
• Enzyme Commision number: 6.4.1.1: pyruvate 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	MN	C	D572 K741 H771 H773	D540 K710 H739 H741
BS02	PYR	C	Q575 L642 T908	Q543 L610 T874
BS03	ATP	C	K152 M192 K194 G198 G199 M204 Y238 I239 H244 Q268 H271 K273 E311 L313 E324 T478	K117 M157 K159 G163 G164 M169 Y203 I204 H209 Q233 H236 K238 E276 L278 E288 T445
BS04	BTI	C	D613 R644 Y651 Q870 T908 S911 K912	D581 R612 Y619 Q836 T874 S877 K878

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004736 pyruvate carboxylase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006090 pyruvate metabolic process
• GO:0006094 gluconeogenesis

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3bg5, PDBe:3bg5, PDBj:3bg5
• PDBsum: 3bg5
• PubMed: 18297087
• UniProt: A0A0H3JRU9|PYC_STAAM Pyruvate carboxylase (Gene Name=pycA)