Structure of PDB 4buc Chain A

Receptor sequence
>4bucA (length=427) Species: 2336 (Thermotoga maritima) [Search protein sequence]
PRGSHMKIGFLGFGKSNRSLLKYLLNHQEAKFFVSEAKTLDGETKKFLEE
HSVEYEEGGHTEKLLDCDVVYVSPGIKPDTSMIELLSSRGVKLSTELQFF
LDNVDPKKVVGITGTDGKSTATALMYHVLSGRGFKTFLGGNFGTPAVEAL
EGEYDYYVLEMSSFQLFWSERPYLSNFLVLNISEDHLDWHSSFKEYVDSK
LKPAFLQTEGDLFVYNKHIERLRNLEGVRSRKIPFWTDENFATEKELIVR
GKKYTLPGNYPYQMRENILAVSVLYMEMFNELESFLELLRDFKPLPHRME
YLGQIDGRHFYNDSKATSTHAVLGALSNFDKVVLIMCGIGKKENYSLFVE
KASPKLKHLIMFGEISKELAPFVGKIPHSIVENMEEAFEKAMEVSEKGDV
ILLSPGGASFAKRGEHFREIFKRHGGD
3D structure
PDB4buc Mreb and Murg as Scaffolds for the Cytoplasmic Steps of Peptidoglycan Biosynthesis
ChainA
Resolution2.17 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K133 N156 H201
Catalytic site (residue number reindexed from 1) K118 N141 H186
Enzyme Commision number 6.3.2.9: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase.
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 PO3 A S96 M97 S81 M82
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008764 UDP-N-acetylmuramoylalanine-D-glutamate 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:4buc, PDBe:4buc, PDBj:4buc
PDBsum4buc
PubMed23826965
UniProtQ9WY76|MURD_THEMA UDP-N-acetylmuramoylalanine--D-glutamate ligase (Gene Name=murD)

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