Structure of PDB 3hbl Chain B Binding Site BS02

Receptor Information

>3hbl Chain B (length=1074) Species: 158878 (Staphylococcus aureus subsp. aureus Mu50)

QIKKLLVANRGEIAIRIFRAAAELDISTVAIYSNEDKSSLHRYKADESYL
VGSDLGPAESYLNIERIIDVAKQANVDAIHPGYGFLSENEQFARRCAEEG
IKFIGPHLEHLDMFGDKVKARTTAIKADLPVIPIDNPKHIEVQVIGDEHG
NIVHLFERDCSVQRRHQKVVEVAPSVGLSPTLRQRICDAAIQLMENIKYV
NAGTVEFLVSGDEFFFIEVNPRVQVEHTITEMVTGIDIVKTQILVAAGAD
LFGEEINMPQQKDITTLGYAIQCRITTEDPLNDFMPDTGTIIAYRSSGGF
GVRLDAGDGFQGAEISPYYDSLLVKLSTHAISFKQAEEKMVRSLREMRIR
GVKTNIPFLINVMKNKKFTSGDYTTKFIEETPELFDIQPSLDRGTKTLEY
IGNVTINGFPNVEKRPKPDYELASIPTVSSSKIASFSGTKQLLDEVGPKG
VAEWVKKQDDVLLTDTTFRDAHQSLLATRVRTKDMINIASKTADVFKDGF
SLEMWGGATFDVAYNFLKENPWERLERLRKAIPNVLFQMLLRASNAVGYK
NYPDNVIHKFVQESAKAGIDVFRIFDSLNWVDQMKVANEAVQEAGKISEG
TICYTGDILNPERSNIYTLEYYVKLAKELEREGFHILAIKDMAGLLKPKA
AYELIGELKSAVDLPIHLHTHDTSGNGLLTYKQAIDAGVDIIDTAVASMS
GLTSQPSANSLYYALNGFPRHLRTDIEGMESLSHYWSTVRTYYSDFESDI
KSPNTEIYQHEMPGGQYSNLSQQAKSLGLGERFDEVKDMYRRVNFLFGDI
VKVAPSSKVVGDMALYMVQNDLDEQSVITDGYKLDFPESVVSFFKGEIGQ
PVNGFNKDLQAVILKGQEALTARPGEYLEPVDFEKVRELLEEEQQGPVTE
QDIISYVLYPKVYEQYIQTRNQYGNLSLLDTPTFFFGMRNGETVEIEIDK
GKRLIIKLETISEPDENGNRTIYYAMNGQARRIYIKDENVHTNANVKPKA
DKSNPSHIGAQMPGSVTEVKVSVGETVKANQPLLITEAMKMETTIQAPFD
GVIKQVTVNNGDTIATGDLLIEIE

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 B 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 K741 H771 H773
• Binding residue (residue number reindexed from 1): D470 K640 H669 H671
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): K152 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 H139 R165 T204 E206 E218 N220 R222 E226 R274 D470 D576 K640 H669 H671 I692 S698 M699 T738 A804 S806 V818 N820 Q825
• 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)