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14-3-3 sigma with RELA/P65 binding site PS45 and covalently bound TCF521-124

Analyse 14-3-3 sigma with RELA/P65 binding site PS45 and covalently bound TCF521-124 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NK5
Type: protein
Length: 238 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P31947, Q04206
Ligands: UGN, CA

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	229	—	P31947
P	—	protein	9	—	Q04206

Ligands and binding sites

UGN · 1-(4-methylphenyl)sulfonyl-4-(2-methylpropyl)piperazine · ligand · chains A, P
CA · Calcium ion · metal · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7NK5 · 14-3-3 sigma with RelA/p65 binding site pS45 and covalently bound TCF521-124 · the same entry in another collection · chain A against A, TM-score 1.00
P31947 · AlphaFold monomer V2.0 prediction for 14-3-3 protein sigma (P31947) · a predicted model of the same protein · chain A against A, TM-score 0.96
Q04206 · AlphaFold monomer V2.0 prediction for transcription factor P65 (Q04206) · a predicted model of the same protein · chain P against A, TM-score 0.33

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P31947
Every structure of UniProt Q04206
Elsewhere: RCSB PDB 7NK5 · PDBe 7NK5 · UniProt P31947 · UniProt Q04206

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