Structure of PDB 4lis Chain A

Receptor sequence
>4lisA (length=364) Species: 227321 (Aspergillus nidulans FGSC A4) [Search protein sequence]
PSGSVLVTGGTGYIGSFTTLALLEAGYKVVVADNLYNSSAEALNRIELIS
GKKAEFAQLDVTDEAAFDKVFEAHPDIDSVIHFAALKAVGESGEKPLDYY
HVNVYGTICLLRSMVRHNVTNIVFSSSATVYGDATRFPDMIPIPEHCPLG
PTNPYGNTKFAIELAITDVINAQRNNAKKAGNETEAAKWNGALLRYFNPA
GAHPSGIMGEDPQGVPYNLLPLLAQVATGKREKLLVFGDDYASHDGTAIR
DYIHILDLADGHLKALNYLRANNPGVRAWNLGTGRGSTVYEMIRAFSKAV
GRDLPYEVAPRRAGDVLNLTSNPTRANTELGWKAQRTLEQACEDLWLWTK
NNPQGYRQQPPAEL
3D structure
PDB4lis Elucidation of Substrate Specificity in Aspergillus nidulans UDP-Galactose-4-Epimerase.
ChainA
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) S127 A128 T129 Y155 K159
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 UPG A K88 S128 Y156 N219 L236 V237 F238 R251 R313 D316 K87 S127 Y155 N218 L235 V236 F237 R250 R312 D315
BS02 NAD A G13 Y14 I15 D34 N35 N38 S39 D61 V62 F84 A86 K88 S128 Y156 K160 Y197 P200 G12 Y13 I14 D33 N34 N37 S38 D60 V61 F83 A85 K87 S127 Y155 K159 Y196 P199
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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