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Atomic structure of DUSP26

Analyse Atomic structure of DUSP26 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HRF
Type: protein
Length: 611 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein phosphatase 26
EC: 3.1.3.16, 3.1.3.48
UniProt: Q9BV47
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 3 distinct chains · 49% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dual specificity protein phosphatase 26 (EC 3.1.3.16, 3.1.3.48)	protein	154	52% helix, 14% strand	Q9BV47
C	Dual specificity protein phosphatase 26 (EC 3.1.3.16, 3.1.3.48)	protein	153	48% helix, 14% strand	Q9BV47
D	Dual specificity protein phosphatase 26 (EC 3.1.3.16, 3.1.3.48)	protein	150	47% helix, 15% strand	Q9BV47

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	349	0.73	0.85	37	empty
2	313	0.72	0.85	38	empty
3	329	0.71	0.84	42	empty
4	262	0.66	0.83	43	empty
5	58	0.30	0.76	20	empty

Interfaces

5 interfaces between chains.

A–C · 1890 Å² buried · 22 hydrogen bonds · protein-protein
B–D · 1797 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 615 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 78 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 76 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4HRF · Atomic structure of DUSP26 · the same entry in another collection · chain D against D, TM-score 1.00
Q9BV47 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 26 (Q9BV47) · a predicted model of the same protein · chain D against A, TM-score 0.83

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 Q9BV47
Elsewhere: RCSB PDB 4HRF · PDBe 4HRF · UniProt Q9BV47

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