Structure of PDB 3qw4 Chain B

Receptor sequence
>3qw4B (length=445) Species: 5661 (Leishmania donovani) [Search protein sequence]
TMSFFDLLNERAKRSLLCVGLDPRAKTAAAAVEECKRLIEQTHEYAAAYK
PNAAFFEFFGAEGWAALSEVIRAVPAGIPVVLDAKRGDIADTADAYATSA
FKHLNAHAITASPYMGSDSLQPFMRYPDKAVFVLCKTSNKGSNDLQCLRV
GDRYLYEAVAERAEGPWNVNGNVGLVVGATDPVALARVRARAPTLWFLVP
GIGAQGGSLKASLDAGLRADGSGMLINVSRGLARAADPRAAAKELCEEIN
AIRFAKGASVELAKALVDSHCVRFGNFTLKSGKSSPIYIDLRRLVTYPAI
MRLVAREYAKVLRHYKFDRIAGLPYAALPIASAISNEMNVPLIYPRREAA
IEGEYKKGDRVVIIDDLVSTETKVEAIEKLRSAGLEVVSIVVLVDRDMGA
KAFLNKLGYDFEAVVGLHQLLPLWRKSNAITSQQEADVRAFLGQW
3D structure
PDB3qw4 The Leishmania donovani UMP synthase is essential for promastigote viability and has an unusual tetrameric structure that exhibits substrate-controlled oligomerization.
ChainB
Resolution3.0 Å
3D
structure
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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 B D21 K49 N51 T136 S137 P199 Q204 S228 R229 D22 K50 N52 T137 S138 P200 Q205 S229 R230
BS02 U5P B D87 I88 T91 D88 I89 T92
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

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Molecular Function

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Biological Process

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

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