Structure of PDB 5nzi Chain A

Receptor sequence
>5nziA (length=482) Species: 5664 (Leishmania major) [Search protein sequence]
SLSAAAQACVKKMRDAKVNEACIRTFIAQHVMVSKGETGSIPDSAIMPVD
SLDALDSLTIECDNAVLQSTVVLKLNGGLGTGMGLCDAKTLLEVKDGKTF
LDFTALQVQYLRQHCSEHLRFMLMDSFNTSASTKSFLKARYPWLYQVFDS
EVELMQNQVPKILQDTLEPAAWAENPAYEWAPPGHGDIYTALYGSGKLQE
LVEQGYRYMFVSNGDNLGATIDKRVLAYMEKEKIDFLMEVCRRTESDKKG
GHLARQTVYVKGKDGQPDAEKRVLLLRESAQCPKADMESFQDINKYSFFN
TNNLWIRLPVLLETMQEHGGTLPLPVIRNEKTVDSSNSASPKVYQLETAM
GAAIAMFESASAIVVPRFRFAPVKTCADLLALRSDAYVVTDDFRLVLDDR
CHGHPPVVDLDSAHYKMMNGFEKLVQHGVPSLVECKRVTVKGLVQFGAGN
VLTGTVTIENTDSASAFVIPDGAKLNDTTASP
3D structure
PDB5nzi Decoding Allosteric Networks in Biocatalysts: Rational Approach to Therapies and Biotechnologies
ChainA
Resolution2.05 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 2.7.7.9: UTP--glucose-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 UPG A L81 G83 G84 Q162 G190 H191 N219 G256 G257 E284 N306 N308 F376 K380 L75 G77 G78 Q156 G184 H185 N213 G250 G251 E278 N300 N302 F370 K374
Gene Ontology
Molecular Function
GO:0003983 UTP:glucose-1-phosphate uridylyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0070569 uridylyltransferase activity
Biological Process
GO:0005977 glycogen metabolic process
GO:0006011 UDP-glucose metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0031981 nuclear lumen
GO:0097014 ciliary plasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5nzi, PDBe:5nzi, PDBj:5nzi
PDBsum5nzi
PubMed
UniProtQ4QDU3

[Back to BioLiP]