Structure of PDB 3bg5 Chain A

Receptor sequence

>3bg5A (length=1137) Species: 1280 (Staphylococcus aureus)

QIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYL
VGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEG
IKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAE
EAGFPLMIKATSRIVREESELEDAFHRAKSEAEKSFGNSEVYIERYIDNP
KHIEVQVIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRIC
DAAIQLMENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGID
IVKTQILVAAGADLFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPD
TGTIIAYRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLSTHAISFKQAE
EKMVRSLREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDI
QPSLDRGTKTLEYIGNVTINGFPNVEKRPKPDYELASIPTVSSSKIASFS
GTKQLLDEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMIN
IASKTADVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLF
QMLLRASNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVA
NEAVQEAGKISEGTICYTGDILNPERSNIYTLEYYVKLAKELEREGFHIL
AIKDMAGLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDA
GVDIIDTAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWS
TVRTYYSDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVK
DMYRRVNFLFGDIVKVTPSSKVVGDMALYMVQNDLDEQSVITDGYKLDFP
ESVVSFFKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVR
ELLEEEQQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFG
MRNGETVEIEIDKGKRLIIKLETISEPDENGNRTIYYAMNGQARRIYIKD
ENVHTNANVKPKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITE
AMKMETTIQAPFDGVIKQVTVNNGDTIATGDLLIEIE

3D structure

• PDB: 3bg5 Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.
• Chain: A
• 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 S189 H202 R228 T267 E269 E281 N283 R285 E289 R337 D533 D639 K703 H732 H734 I755 S761 M762 T801 T867 S869 V881 N883 Q888
• 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	A	D572 H771 H773	D533 H732 H734
BS02	PYR	A	L642 K741	L603 K703
BS03	ATP	A	K152 M192 K194 Y238 I239 H244 Q268 H271 E311 L313 E324 N326	K117 M157 K159 Y196 I197 H202 Q226 H229 E269 L271 E281 N283
BS04	BTI	A	Y503 G511 F512 P513 F618	Y463 G471 F472 P473 F579

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)