Structure of PDB 1p3d Chain A

Receptor sequence
>1p3dA (length=463) Species: 727 (Haemophilus influenzae) [Search protein sequence]
IIPEMRRVQQIHFIGIGGAGMSGIAEILLNEGYQISGSDIADGVVTQRLA
QAGAKIYIGHAEEHIEGASVVVVSSAIKDDNPELVTSKQKRIPVIQRAQM
LAEIMRFRHGIAVAGTHGKTTTTAMISMIYTQAKLDPTFVNGGLVKSAGK
NAHLGASRYLIAEADESDASFLHLQPMVSVVTNMEPDHMDTYEGDFEKMK
ATYVKFLHNLPFYGLAVMCADDPVLMELVPKVGRQVITYGFSEQADYRIE
DYEQTGFQGHYTVICPNNERINVLLNVPGKHNALNATAALAVAKEEGIAN
EAILEALADFQGAGRRFDQLGEFIRPNGKVRLVDDYGHHPTEVGVTIKAA
REGWGDKRIVMIFQPHRYSRTRDLFDDFVQVLSQVDALIMLDVYAAGEAP
IVGADSKSLCRSIRNLGKVDPILVSDTSQLGDVLDQIIQDGDLILAQGAG
SVSKISRGLAESW
3D structure
PDB1p3d Crystal Structures of Active Fully Assembled Substrate- and Product-Bound Complexes of UDP-N-Acetylmuramic Acid:L-Alanine Ligase (MurC) from Haemophilus influenzae.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K129 T130 L154 E173 H198
Catalytic site (residue number reindexed from 1) K119 T120 L144 E163 H188
Enzyme Commision number 6.3.2.8: UDP-N-acetylmuramate--L-alanine ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008763 UDP-N-acetylmuramate-L-alanine 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1p3d, PDBe:1p3d, PDBj:1p3d
PDBsum1p3d
PubMed12837790
UniProtP45066|MURC_HAEIN UDP-N-acetylmuramate--L-alanine ligase (Gene Name=murC)

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