Structure of PDB 4lis Chain B

Receptor sequence
>4lisB (length=363) Species: 227321 (Aspergillus nidulans FGSC A4) [Search protein sequence]
SGSVLVTGGTGYIGSFTTLALLEAGYKVVVADNLYNSSAEALNRIELISG
KKAEFAQLDVTDEAAFDKVFEAHPDIDSVIHFAALKAVGESGEKPLDYYH
VNVYGTICLLRSMVRHNVTNIVFSSSATVYGDATRFPDMIPIPEHCPLGP
TNPYGNTKFAIELAITDVINAQRNNAKKAGNETEAAKWNGALLRYFNPAG
AHPSGIMGEDPQGVPYNLLPLLAQVATGKREKLLVFGDDYASHDGTAIRD
YIHILDLADGHLKALNYLRANNPGVRAWNLGTGRGSTVYEMIRAFSKAVG
RDLPYEVAPRRAGDVLNLTSNPTRANTELGWKAQRTLEQACEDLWLWTKN
NPQGYRQQPPAEL
3D structure
PDB4lis Elucidation of Substrate Specificity in Aspergillus nidulans UDP-Galactose-4-Epimerase.
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S128 A129 T130 Y156 K160
Catalytic site (residue number reindexed from 1) S126 A127 T128 Y154 K158
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 UDP B N199 N219 L220 L236 V237 F238 R251 V290 R313 D316 N197 N217 L218 L234 V235 F236 R249 V288 R311 D314
BS02 NAD B G13 Y14 I15 D34 N35 N38 S39 D61 V62 F84 A86 K88 S128 Y156 K160 Y197 P200 G11 Y12 I13 D32 N33 N36 S37 D59 V60 F82 A84 K86 S126 Y154 K158 Y195 P198
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003978 UDP-glucose 4-epimerase activity
GO:0016853 isomerase activity
Biological Process
GO:0006012 galactose metabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4lis, PDBe:4lis, PDBj:4lis
PDBsum4lis
PubMed24116166
UniProtC8VAU8

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