Structure of PDB 3hbl Chain A Binding Site BS01

Receptor Information

>3hbl Chain A (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

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 3hbl Chain A Residue 2002

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3hbl A Symmetrical Tetramer for S. aureus Pyruvate Carboxylase in Complex with Coenzyme A.
• Resolution: 2.71 Å
• Binding residue (original residue number in PDB): D572 H771 H773
• Binding residue (residue number reindexed from 1): D527 H726 H728
• Annotation score: 1

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.

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)