Structure of PDB 6c4j Chain F Binding Site BS02
Receptor Information
>6c4j Chain F (length=460) Species:
9606
(Homo sapiens) [
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MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTL
PIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGK
GRALDLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKP
NLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYE
HWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEE
VATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYW
QQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSS
IYISKYLMDEGAHLHIYDPKVPREQIVVDLSHDQVSRLVTISKDPYEACD
GAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIG
FQIETIGKKV
Ligand information
Ligand ID
UPG
InChI
InChI=1S/C15H24N2O17P2/c18-3-5-8(20)10(22)12(24)14(32-5)33-36(28,29)34-35(26,27)30-4-6-9(21)11(23)13(31-6)17-2-1-7(19)16-15(17)25/h1-2,5-6,8-14,18,20-24H,3-4H2,(H,26,27)(H,28,29)(H,16,19,25)/t5-,6-,8-,9-,10+,11-,12-,13-,14-/m1/s1
InChIKey
HSCJRCZFDFQWRP-JZMIEXBBSA-N
SMILES
Software
SMILES
CACTVS 3.370
OC[C@H]1O[C@H](O[P](O)(=O)O[P](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 12.01
O=C1C=CN(C(=O)N1)C2OC(C(O)C2O)COP(=O)(OP(=O)(OC3OC(C(O)C(O)C3O)CO)O)O
CACTVS 3.370
OC[CH]1O[CH](O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6
C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@](=O)(O)O[P@](=O)(O)O[C@@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O)O)O
OpenEye OEToolkits 1.7.6
C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OC3C(C(C(C(O3)CO)O)O)O)O)O
Formula
C15 H24 N2 O17 P2
Name
URIDINE-5'-DIPHOSPHATE-GLUCOSE;
URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE ESTER
ChEMBL
CHEMBL375951
DrugBank
DB01861
ZINC
ZINC000008215472
PDB chain
6c4j Chain F Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
6c4j
Hysteresis and Allostery in Human UDP-Glucose Dehydrogenase Require a Flexible Protein Core.
Resolution
2.53 Å
Binding residue
(original residue number in PDB)
F162 L163 A164 E165 K220 N224 I231 F265 K267 S269 F272 G273 C276 F277 F338 K339 R442
Binding residue
(residue number reindexed from 1)
F162 L163 A164 E165 K220 N224 I231 F265 K267 S269 F272 G273 C276 F277 F338 K339 R436
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
T131 E165 K220 N224 C276 D280
Catalytic site (residue number reindexed from 1)
T131 E165 K220 N224 C276 D280
Enzyme Commision number
1.1.1.22
: UDP-glucose 6-dehydrogenase.
Gene Ontology
Molecular Function
GO:0003979
UDP-glucose 6-dehydrogenase activity
GO:0016491
oxidoreductase activity
GO:0016616
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042802
identical protein binding
GO:0051287
NAD binding
Biological Process
GO:0001702
gastrulation with mouth forming second
GO:0006024
glycosaminoglycan biosynthetic process
GO:0006065
UDP-glucuronate biosynthetic process
GO:0015012
heparan sulfate proteoglycan biosynthetic process
GO:0030206
chondroitin sulfate biosynthetic process
GO:0034214
protein hexamerization
GO:0048666
neuron development
Cellular Component
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005829
cytosol
GO:0070062
extracellular exosome
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6c4j
,
PDBe:6c4j
,
PDBj:6c4j
PDBsum
6c4j
PubMed
30457329
UniProt
O60701
|UGDH_HUMAN UDP-glucose 6-dehydrogenase (Gene Name=UGDH)
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