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The structure of the rhodanese domain of the human dual specificity phosphatase 16

Analyse The structure of the rhodanese domain of the human dual specificity phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VSW
Type: protein
Length: 268 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein phosphatase 16
UniProt: Q9BY84
Pockets: 3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dual specificity protein phosphatase 16	protein	134	41% helix, 17% strand	Q9BY84

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.43	0.79	20	empty
2	94	0.40	0.76	25	empty
3	74	0.33	0.75	22	empty

Interfaces

1 interface between chains.

A–B · 558 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2VSW · The structure of the rhodanese domain of the human dual specificity phosphatase 16 · the same entry in another collection · chain A against A, TM-score 1.00
Q9BY84 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 16 (Q9BY84) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q9BY84
Elsewhere: RCSB PDB 2VSW · PDBe 2VSW · UniProt Q9BY84

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