Structure of PDB 2xja Chain C

Receptor sequence
>2xjaC (length=498) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
RPNAVVGVRLAALADQVGAALVTEDRTVTGVTLRAQDVSPGDLFAALTGS
TTHGARHVGDAIARGAVAVLTDPAGVAEIAGRAAVPVLVHPAPRGVLGGL
AATVYGHPSERLTVIGITGTSGKTTTTYLVEAGLRAAGRVAGLIGTIGIR
VGGADLPSALTTPEAPTLQAMLAAMVERGVDTVVMEVSSHALALGRVDGT
RFAVGAFTNLSRDHLDFHPSMADYFEAKASLFDPDSALRARTAVVCIDDD
AGRAMAARAADAITVSAADRPAHWRATDVAPTDAGGQQFTAIDPAGVGHH
IGIRLPGRYNVANCLVALAILDTVGVSPEQAVPGLREIRVPGRLEQIDRG
QGFLALVDYAHKPEALRSVLTTLAHPDRRLAVVFGAGGDRDPGKRAPMGR
IAAQLADLVVVTDDNPRDEDPTAIRREILAGAAEVGGDAQVVEIADRRDA
IRHAVAWARPGDVVLIAGKGHETGQRGGGRVRPFDDRVELAAALEALE
3D structure
PDB2xja Essential Residues for the Enzyme Activity of ATP-Dependent Mure Ligase from Mycobacterium Tuberculosis.
ChainC
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K157 T158
Catalytic site (residue number reindexed from 1) K123 T124
Enzyme Commision number 6.3.2.13: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0008765 UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity
GO:0016874 ligase activity
GO:0016881 acid-amino acid ligase activity
Biological Process
GO:0008360 regulation of cell shape
GO:0009058 biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2xja, PDBe:2xja, PDBj:2xja
PDBsum2xja
PubMed21153518
UniProtP9WJL3|MURE_MYCTU UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (Gene Name=murE)

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