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Crystal structure of the tasor pseudo-parp domain

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

PDB: 6TL1
Type: protein
Length: 412 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein tasor
UniProt: Q9UK61
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein tasor	protein	210	24% helix, 27% strand	Q9UK61
B	Protein tasor	protein	202	24% helix, 27% strand	Q9UK61

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1029	0.75	0.78	70	empty
2	109	0.47	0.79	22	empty
3	61	0.46	0.83	15	empty
4	79	0.38	0.77	16	empty
5	74	0.37	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 506 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6TL1 · Crystal structure of the TASOR pseudo-PARP domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9UK61 · AlphaFold monomer V2.0 prediction for protein tasor (Q9UK61) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q9UK61
Elsewhere: RCSB PDB 6TL1 · PDBe 6TL1 · UniProt Q9UK61

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