Structure of PDB 4bqh Chain A

Receptor sequence

>4bqhA (length=521) Species: 5691 (Trypanosoma brucei)

PLGSMSDRDVCIQRLTGANQDHILTALEHGSEAERASLTAQITNELAGVD
FRHFNDVLRESLEISKSLAEPPAKDSFFDISSVDRRRGQAKRIKNLEAVG
YKAIQKGQIAFLILAGGSGTRLGFDKPKGFFTCDGLQQRKSLFMMHCEKI
RRRQEIAESISGSGRKARVQLLVMTSGQNDAETQRFFEENSYFGLEREQV
HFFAQSSVPCYDENTGRIIMENRGRICAAPGGNGAVFAALAAPRATKTLQ
VKESLLQHLRKLGIAYVQIGNIDNLLANVADPVFIGYAIEEEAHVVVKTC
PKRGPDERVGVFVRASGKWGVVEYTEIRAKEIDDATGELKFNCANISSNL
CSLHFMSLAAERMKSFTQYHAARKKIPTIKGPVMGIKLEAFLFDLFRFVD
ECDHPPKDSGAFRIMQVDRDDEFGPVKNADGAASDTPADAVRLLLSQHTR
WLITALETAAMGVDVTEAKEAVAVMRSCSIKAEISPLVSVGGEGLRQHLP
RVIHQLLRNPPPVIFIRRDDE

3D structure

• PDB: 4bqh A Novel Allosteric Inhibitor of the Uridine Diphosphate N-Acetylglucosamine Pyrophosphorylase from Trypanosoma Brucei.
• Chain: A
• Resolution: 1.75 Å

Enzymatic activity

• Enzyme Commision number: 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	9VU	A	G44 V45 D46 F50 V209 G232 A236 A239 M370 K371 Y376	G48 V49 D50 F54 V208 G231 A235 A238 M363 K364 Y369	MOAD: Kd=2.58uM PDBbind-CN: -logKd/Ki=5.59,Kd=2.58uM

Gene Ontology

Molecular Function

• GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity
• GO:0016740 transferase activity
• GO:0016779 nucleotidyltransferase activity
• GO:0070569 uridylyltransferase activity

Biological Process

• GO:0006011 UDP-glucose metabolic process
• GO:0006048 UDP-N-acetylglucosamine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0020015 glycosome

External links

• PDB: RCSB:4bqh, PDBe:4bqh, PDBj:4bqh
• PDBsum: 4bqh
• PubMed: 23834437
• UniProt: Q386Q8