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Crystal structure of DUSP15

Analyse Crystal structure of DUSP15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YZ4
Type: protein
Length: 315 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity phosphatase-like 15 isoform a
EC: 3.1.3.48
UniProt: Q5QP65
Ligands: SO4
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity phosphatase-like 15 isoform a (EC 3.1.3.48)	protein	159	47% helix, 14% strand	Q5QP65
B	Dual specificity phosphatase-like 15 isoform a (EC 3.1.3.48)	protein	156	48% helix, 13% strand	Q5QP65

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B
BOG · octyl beta-D-glucopyranoside · additive · chains A

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

Pockets

3 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	339	0.70	0.83	42	empty
2	108	0.52	0.82	22	empty
3	59	0.29	0.74	12	empty

Interfaces

1 interface between chains.

A–B · 665 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

1YZ4 · Crystal structure of DUSP15 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q5QP65
Elsewhere: RCSB PDB 1YZ4 · PDBe 1YZ4 · UniProt Q5QP65

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