Structure of PDB 1ek6 Chain A Binding Site BS01

Receptor Information
>1ek6 Chain A (length=346) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLR
RVQELTGRSVEFEEMDILDQGALQRLFKKYSFMAVIHFAGLKAVGESVQK
PLDYYRVNLTGTIQLLEIMKAHGVKNLVFSSSATVYGNPQYLPLDEAHPT
GGCTNPYGKSKFFIEEMIRDLCQADKTWNAVLLRYFNPTGAHASGCIGED
PQGIPNNLMPYVSQVAIGRREALNVFGNDYDTEDGTGVRDYIHVVDLAKG
HIAALRKLKEQCGCRIYNLGTGTGYSVLQMVQAMEKASGKKIPYKVVARR
EGDVAACYANPSLAQEELGWTAALGLDRMCEDLWRWQKQNPSGFGT
Ligand information
Ligand IDNAI
InChIInChI=1S/C21H29N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1,3-4,7-8,10-11,13-16,20-21,29-32H,2,5-6H2,(H2,23,33)(H,34,35)(H,36,37)(H2,22,24,25)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBOPGDPNILDQYTO-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=CCC(=C5)C(=O)N)O)O)O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[C@@H]2O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)N5C=CCC(=C5)C(=O)N)O)O)O)O)N
CACTVS 3.341NC(=O)C1=CN(C=CC1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
FormulaC21 H29 N7 O14 P2
Name1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE;
NADH
ChEMBLCHEMBL1234616
DrugBankDB00157
ZINCZINC000008215403
PDB chain1ek6 Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ek6 Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		G9 G12 Y13 I14 D33 N34 H36 N37 D66 I67 F88 A89 G90 K92 S130 S131 S132 Y157 K161 Y185 P188
Binding residue
(residue number reindexed from 1)		G9 G12 Y13 I14 D33 N34 H36 N37 D66 I67 F88 A89 G90 K92 S130 S131 S132 Y157 K161 Y185 P188
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S132 A133 T134 Y157 K161
Catalytic site (residue number reindexed from 1) S132 A133 T134 Y157 K161
Enzyme Commision number 5.1.3.2: UDP-glucose 4-epimerase.
5.1.3.7: UDP-N-acetylglucosamine 4-epimerase.
Gene Ontology
Molecular Function
GO:0003974 UDP-N-acetylglucosamine 4-epimerase activity
GO:0003978 UDP-glucose 4-epimerase activity
GO:0016853 isomerase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006012 galactose metabolic process
GO:0019388 galactose catabolic process
GO:0033499 galactose catabolic process via UDP-galactose
Cellular Component
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:1ek6, PDBe:1ek6, PDBj:1ek6
PDBsum1ek6
PubMed10801319
UniProtQ14376|GALE_HUMAN UDP-glucose 4-epimerase (Gene Name=GALE)

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