Structure of PDB 7bkh Chain A Binding Site BS02

Receptor Information
>7bkh Chain A (length=227) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVA
YKNVVGGQRAAWRVLSSIEQKSNGPEVREYREKVETELQGVCDTVLGLLD
SHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEA
MDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMAD
LHTLSEDSYKDSTLIMQLLRDNLTLWT
Ligand information
Ligand IDU1B
InChIInChI=1S/C12H14N2O4/c15-8-9-3-4-11(14(17)18)12(6-9)13-5-1-2-10(16)7-13/h3-4,6,8,10,16H,1-2,5,7H2/t10-/m0/s1
InChIKeyGGOBRMGVXJGMTC-JTQLQIEISA-N
SMILES
SoftwareSMILES
CACTVS 3.385O[CH]1CCCN(C1)c2cc(C=O)ccc2[N](=O)=O
OpenEye OEToolkits 2.0.7c1cc(c(cc1C=O)N2CCCC(C2)O)N(=O)=O
OpenEye OEToolkits 2.0.7c1cc(c(cc1C=O)N2CCC[C@@H](C2)O)N(=O)=O
CACTVS 3.385O[C@H]1CCCN(C1)c2cc(C=O)ccc2[N](=O)=O
FormulaC12 H14 N2 O4
Name4-nitro-3-[(3S)-3-oxidanylpiperidin-1-yl]benzaldehyde;
4-nitro-3-[(3~{S})-3-oxidanylpiperidin-1-yl]benzaldehyde;
3-(3-hydroxypiperidin-1-yl)-4-nitrobenzaldehyde
ChEMBL
DrugBank
ZINC
PDB chain7bkh Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB7bkh An Exploration of Chemical Properties Required for Cooperative Stabilization of the 14-3-3 Interaction with NF-kappa B-Utilizing a Reversible Covalent Tethering Approach.
Resolution1.4 Å
Binding residue
(original residue number in PDB)		V46 K122 P167 I219
Binding residue
(residue number reindexed from 1)		V49 K118 P163 I215
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008426 protein kinase C inhibitor activity
GO:0019901 protein kinase binding
GO:0042802 identical protein binding
GO:0045296 cadherin binding
GO:0050815 phosphoserine residue binding
GO:0051219 phosphoprotein binding
GO:0140311 protein sequestering activity
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0001836 release of cytochrome c from mitochondria
GO:0003334 keratinocyte development
GO:0006469 negative regulation of protein kinase activity
GO:0006611 protein export from nucleus
GO:0007165 signal transduction
GO:0008104 protein localization
GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage
GO:0010482 regulation of epidermal cell division
GO:0010839 negative regulation of keratinocyte proliferation
GO:0022407 regulation of cell-cell adhesion
GO:0030216 keratinocyte differentiation
GO:0030307 positive regulation of cell growth
GO:0031424 keratinization
GO:0032880 regulation of protein localization
GO:0043588 skin development
GO:0043616 keratinocyte proliferation
GO:0045606 positive regulation of epidermal cell differentiation
GO:0045785 positive regulation of cell adhesion
GO:0045824 negative regulation of innate immune response
GO:0046827 positive regulation of protein export from nucleus
GO:0051726 regulation of cell cycle
GO:0061436 establishment of skin barrier
GO:0072089 stem cell proliferation
GO:0141156 cAMP/PKA signal transduction
GO:1903077 negative regulation of protein localization to plasma membrane
GO:1903829 positive regulation of protein localization
GO:2000647 negative regulation of stem cell proliferation
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7bkh, PDBe:7bkh, PDBj:7bkh
PDBsum7bkh
PubMed34076416
UniProtP31947|1433S_HUMAN 14-3-3 protein sigma (Gene Name=SFN)

[Back to BioLiP]