Structure of PDB 3hbl Chain A

Receptor sequence

>3hblA (length=1131) Species: 158878 (Staphylococcus aureus subsp. aureus Mu50)

QIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYL
VGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEG
IKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPGTDGPIKSYELAKEFAE
EAGFPLMIKATSRIVREESELEDAFHRAKSEAEEVYIERYIDNPKHIEVQ
VIGDEHGNIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRICDAAIQL
MENIKYVNAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQI
LVAAGADLFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIA
YRSSGGFGVRLDAGDGFQGAEISPYYDSLLVKLSTHAISFKQAEEKMVRS
LREMRIRGVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDIQPSLDR
GTKTLEYIGNVTINGFPNVEKRPKPDYELASIPTVSSSKIASFSGTKQLL
DEVGPKGVAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMINIASKTA
DVFKDGFSLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLRA
SNAVGYKNYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQE
AGKISEGTICYTGDILNPERSNIYTLEYYVKLAKELEREGFHILAIKDMA
GLLKPKAAYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIID
TAVASMSGLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYY
SDFESDIKSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRV
NFLFGDIVKVAPSSKVVGDMALYMVQNDLDEQSVITDGYKLDFPESVVSF
FKGEIGQPVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVRELLEEE
QQGPVTEQDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGMRNGET
VEIEIDKGKRLIIKLETISEPDENGNRTIYYAMNGQARRIYIKDENVHTN
ANVKPKADKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMET
TIQAPFDGVIKQVTVNNGDTIATGDLLIEIE

3D structure

• PDB: 3hbl A Symmetrical Tetramer for S. aureus Pyruvate Carboxylase in Complex with Coenzyme A.
• Chain: A
• Resolution: 2.71 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K152 K194 H244 R270 T309 E311 E324 N326 R328 E332 R377 D572 D678 K741 H771 H773 I794 S800 M801 T840 A908 S910 V922 N924 Q929
• Catalytic site (residue number reindexed from 1): K117 K159 H196 R222 T261 E263 E275 N277 R279 E283 R331 D527 D633 K697 H726 H728 I749 S755 M756 T795 A861 S863 V875 N877 Q882
• 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	D527 H726 H728
BS02	BTI	A	N506 G511 F512 F618 K620	N460 G465 F466 F573 K575

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:3hbl, PDBe:3hbl, PDBj:3hbl
• PDBsum: 3hbl
• PubMed: 19523900
• UniProt: A0A0H3JRU9|PYC_STAAM Pyruvate carboxylase (Gene Name=pycA)