Structure of PDB 4kql Chain A

Receptor sequence
>4kqlA (length=450) Species: 727 (Haemophilus influenzae) [Search protein sequence]
KALSAVILAAGKGTRMYSDLPKVLHTIAGKPMVKHVIDTAHQLGSENIHL
IYGHGGDLMRTHLANEQVNWVLQTEQLGTAHAVQQAAPFFKDNENIVVLY
GDAPLITKETLEKLIEAKPENGIALLTVNLDNPTGYGRIIRENGNVVAIV
EQKDANAEQLNIKEVNTGVMVSDGASFKKWLARVGNNNAQGEYYLTDLIA
LANQDNCQVVAVQATDVMEVEGANNRLQLAALERYFQNKQASKLLLEGVM
IYDPARFDLRGTLEHGKDVEIDVNVIIEGNVKLGDRVKIGTGCVLKNVVI
GNDVEIKPYSVLEDSIVGEKAAIGPFSRLRPGAELAAETHVGNFVEIKKS
TVGKGSKVNHLTYVGDSEIGSNCNIGAGVITCNYDGANKFKTIIGDDVFV
GSDTQLVAPVKVANGATIGAGTTITRDVGENELVITRVAQRHIQGWQRPI
3D structure
PDB4kql Rational design of inhibitors of the bacterial cell wall synthetic enzyme GlmU using virtual screening and lead-hopping.
ChainA
Resolution2.31 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) R18
Catalytic site (residue number reindexed from 1) R15
Enzyme Commision number 2.3.1.157: glucosamine-1-phosphate N-acetyltransferase.
2.7.7.23: UDP-N-acetylglucosamine diphosphorylase.
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 1SG A A12 A13 Q76 Q79 G81 T82 Y103 D105 Y139 T170 V223 G225 A9 A10 Q73 Q76 G78 T79 Y100 D102 Y136 T167 V220 G222 MOAD: ic50=0.0017uM
PDBbind-CN: -logKd/Ki=8.77,IC50=0.0017uM
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0000902 cell morphogenesis
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0008360 regulation of cell shape
GO:0009245 lipid A biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4kql, PDBe:4kql, PDBj:4kql
PDBsum4kql
PubMed25262942
UniProtP43889|GLMU_HAEIN Bifunctional protein GlmU (Gene Name=glmU)

[Back to BioLiP]