Research workbench

Structure of 53BP1 tandem tudor domains in complex with small molecule UNC2991

Analyse Structure of 53BP1 tandem tudor domains in complex with small molecule UNC2991 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MXX
Type: protein
Length: 1,196 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q12888
Ligands: K6P, PO4

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D, E, F	—	protein	120	—	Q12888
B, G, H	—	protein	119	—	Q12888
C	—	protein	121	—	Q12888
I	—	protein	118	—	Q12888
J	—	protein	120	—	Q12888

Ligands and binding sites

K6P · N-[3-(tert-butylamino)propyl]-3-iodobenzamide · ligand · 5 copies · chains A, B, C, D, E, F, G, H, I, J
PO4 · Phosphate ion · ion · 21 copies · chains A, B, D, C, E, F, G, H, I, J
FMT · Formic acid · additive · 4 copies · chains B, H, G

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

Compared structures

6MXX · Structure of 53BP1 tandem Tudor domains in complex with small molecule UNC2991 · the same entry in another collection · chain J against J, TM-score 1.00
Q12888 · AlphaFold monomer V2.0 prediction for TP53-binding protein 1 (Q12888) · a predicted model of the same protein · chain I against A, TM-score 0.95

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 Q12888
Elsewhere: RCSB PDB 6MXX · PDBe 6MXX · UniProt Q12888

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.