Structure of PDB 4y7v Chain A

Receptor sequence
>4y7vA (length=216) Species: 931281 (Pseudomonas putida BIRD-1) [Search protein sequence]
MKAMILAAGKGERMRPLTLHTPKPLVPVAGQPLIEYHLRALAAAGVTEVV
INHAWLGQQIEDHLGDGSRFGLSIRYSPEGEPLETGGGIFKALPLLGDAP
FLLVNGDVWTDYDFARLQAPLQGLAHLVLVDNPGRGDFRLVGEQVVDGDD
GTLTFSGISVLHPALFEGCQAGAFKLAPLLRQAMAAGKVSGEHYRGHWVD
VGTLERLAEAESLIGE
3D structure
PDB4y7v Crystal Structure of the N-Acetylmuramic Acid alpha-1-Phosphate (MurNAc-alpha 1-P) Uridylyltransferase MurU, a Minimal Sugar Nucleotidyltransferase and Potential Drug Target Enzyme in Gram-negative Pathogens.
ChainA
Resolution1.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.7.7.99: N-acetyl-alpha-D-muramate 1-phosphate uridylyltransferase.
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 491 A N105 D140 F160 W203 D205 N105 D137 F155 W198 D200
BS02 2PN A G9 K10 G11 E12 R13 K23 G9 K10 G11 E12 R13 K23
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0002134 UTP binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0070569 uridylyltransferase activity
GO:0097367 carbohydrate derivative binding
Biological Process
GO:0008360 regulation of cell shape
GO:0009058 biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0009254 peptidoglycan turnover
GO:0046677 response to antibiotic
GO:0071555 cell wall organization
GO:0097172 N-acetylmuramic acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4y7v, PDBe:4y7v, PDBj:4y7v
PDBsum4y7v
PubMed25767118
UniProtQ88QT2|MURU_PSEPK N-acetylmuramate alpha-1-phosphate uridylyltransferase (Gene Name=murU)

[Back to BioLiP]