Structure of PDB 4twr Chain A

Receptor sequence
>4twrA (length=325) Species: 359391 (Brucella abortus 2308) [Search protein sequence]
ANNVLVVGGAGFIGSHTAKLLAGQGYAPVVYDNLSTGHQSAVRWGDFVEG
DILDQARLVETMEKYAPVAVIHFAASAYVGESVEDPAKYYRNNVGGTQSL
LDACRLTRTQNVIFSSSCATYGVPSRLPIGEGEAQNPINPYGRTKLIAEH
MLADYAVAYGLRYVALRYFNASGADIDGELGEKHDPETHLIPRAMMAAAG
RLDVLEVYGDDYETPDGTCIRDYIHVTDLARAHVLAVEHLKEAGGNLAVN
LGTGRGTSIREIVQSIGRLTGRSVPVAMRARRAGDPPALYADPALAAEKL
GFHTVYSDLDTIIRTAAPHFGLEVR
3D structure
PDB4twr Structure of UDP-glucose 4-epimerase from Brucella melitensis
ChainA
Resolution1.9 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) S119 C120 A121 Y143 K147 H186 H191
Catalytic site (residue number reindexed from 1) S117 C118 A119 Y141 K145 H184 H189
Enzyme Commision number 5.1.3.2: UDP-glucose 4-epimerase.
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 NAD A G10 G13 F14 I15 D34 N35 L36 S37 T38 G39 D53 I54 F75 A76 A77 N94 S117 K147 Y170 A173 H186 G8 G11 F12 I13 D32 N33 L34 S35 T36 G37 D51 I52 F73 A74 A75 N92 S115 K145 Y168 A171 H184
BS02 ZN A E184 H186 E189 H191 E182 H184 E187 H189
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003978 UDP-glucose 4-epimerase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0006012 galactose metabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4twr, PDBe:4twr, PDBj:4twr
PDBsum4twr
PubMed
UniProtQ2YKG6

[Back to BioLiP]