Structure of PDB 3qw4 Chain C

Receptor sequence
>3qw4C (length=447) Species: 5661 (Leishmania donovani) [Search protein sequence]
TMSFFDLLNERAKRSLLCVGLDPRAKTAAAAVEECKRLIEQTHEYAAAYK
PNAAFFEFFGAEGWAALSEVIRAVPAGIPVVLDAKRGDIADTADAYATSA
FKHLNAHAITASPYMGSDSLQPFMRYPDKAVFVLCKTSNKGSNDLQCLRV
GDRYLYEAVAERAEGPWNVNGNVGLVVGATDPVALARVRARAPTLWFLVP
GIGAQGGSLKASLDAGLRADGSGMLINVSRGLARAADPRAAAKELCEEIN
AIRFKGASVELAKALVDSHCVRFGNFTLKSGKSSPIYIDLRRLVTYPAIM
RLVAREYAKVLRHYKFDRIAGLPYAALPIASAISNEMNVPLIYPRREAKA
AIEGEYKKGDRVVIIDDLVSTGETKVEAIEKLRSAGLEVVSIVVLVDRDM
GAKAFLNKLGYDFEAVVGLHQLLPLWRKSNAITSQQEADVRAFLGQW
3D structure
PDB3qw4 The Leishmania donovani UMP synthase is essential for promastigote viability and has an unusual tetrameric structure that exhibits substrate-controlled oligomerization.
ChainC
Resolution3.0 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 4.1.1.23: orotidine-5'-phosphate decarboxylase.
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 U5P C D87 I88 T91 D88 I89 T92
BS02 U5P C K279 Y287 I288 R291 D371 D372 L373 S375 G377 E378 T379 R403 K279 Y287 I288 R291 D366 D367 L368 S370 G372 E373 T374 R398
BS03 U5P C D21 K49 D82 T136 S137 P199 S228 R229 D22 K50 D83 T137 S138 P200 S229 R230
Gene Ontology
Molecular Function
GO:0004588 orotate phosphoribosyltransferase activity
GO:0004590 orotidine-5'-phosphate decarboxylase activity
GO:0016757 glycosyltransferase activity
GO:0016831 carboxy-lyase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3qw4, PDBe:3qw4, PDBj:3qw4
PDBsum3qw4
PubMed21507942
UniProtH9ABT8

[Back to BioLiP]