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Crystal structure of human DUSP5

Analyse Crystal structure of human DUSP5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2G6Z
Type: protein
Length: 436 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein phosphatase 5
EC: 3.1.3.48, 3.1.3.16
UniProt: Q16690
Ligands: SO4
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity protein phosphatase 5 (EC 3.1.3.48, 3.1.3.16)	protein	147	45% helix, 15% strand	Q16690
B	Dual specificity protein phosphatase 5 (EC 3.1.3.48, 3.1.3.16)	protein	143	46% helix, 16% strand	Q16690
C	Dual specificity protein phosphatase 5 (EC 3.1.3.48, 3.1.3.16)	protein	146	45% helix, 16% strand	Q16690

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B, C

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	649	0.69	0.78	73	empty

Interfaces

3 interfaces between chains.

B–C · 870 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 501 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 68 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

2G6Z · Crystal structure of human DUSP5 · the same entry in another collection · chain C against C, TM-score 1.00
Q16690 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 5 (Q16690) · 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 Q16690
Elsewhere: RCSB PDB 2G6Z · PDBe 2G6Z · UniProt Q16690

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