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Crystal structure of the tpr domain of SMG6

Analyse Crystal structure of the tpr domain of SMG6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UM2
Type: protein
Length: 510 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Telomerase-binding protein EST1A
EC: 3.1.-.-
UniProt: Q86US8
Pockets: 5 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Telomerase-binding protein EST1A (EC 3.1.-.-)	protein	510	69% helix, 4% strand	Q86US8

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	295	0.61	0.79	33	empty
2	154	0.56	0.81	23	GOL
3	99	0.39	0.76	22	empty
4	101	0.38	0.75	17	empty
5	80	0.31	0.73	19	empty

Compared structures

4UM2 · Crystal structure of the TPR domain of SMG6 · the same entry in another collection · chain A against A, TM-score 1.00
Q86US8 · AlphaFold monomer V2.0 prediction for telomerase-binding protein EST1A (Q86US8) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q86US8
Elsewhere: RCSB PDB 4UM2 · PDBe 4UM2 · UniProt Q86US8

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