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Human tyrosyl DNA phosphodiesterase

Analyse Human tyrosyl DNA phosphodiesterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QZQ
Type: protein
Length: 876 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosyl-DNA phosphodiesterase 1
UniProt: Q9NUW8
Pockets: 7 · best druggability 0.59

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosyl-DNA phosphodiesterase 1	protein	439	27% helix, 24% strand	Q9NUW8
B	Tyrosyl-DNA phosphodiesterase 1	protein	437	28% helix, 24% strand	Q9NUW8

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	399	0.59	0.75	52	empty
2	187	0.53	0.79	23	empty
3	246	0.52	0.76	31	empty
4	134	0.50	0.79	22	empty
5	130	0.48	0.78	24	empty

Interfaces

1 interface between chains.

A–B · 413 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1QZQ · human Tyrosyl DNA phosphodiesterase · the same entry in another collection · chain A against A, TM-score 1.00
Q9NUW8 · AlphaFold monomer V2.0 prediction for tyrosyl-DNA phosphodiesterase 1 (Q9NUW8) · 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 Q9NUW8
Elsewhere: RCSB PDB 1QZQ · PDBe 1QZQ · UniProt Q9NUW8

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