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Crystal structure of D1 and D2 catalytic domains of human protein tyrosine phosphatase gamma (D1+D2 ptprg)

Analyse Crystal structure of D1 and D2 catalytic domains of human protein tyrosine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NLK
Type: protein
Length: 553 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein tyrosine phosphatase, receptor type, G variant (fragment)
EC: 3.1.3.48
UniProt: Q59EE0
Pockets: 10 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein tyrosine phosphatase, receptor type, G variant (fragment) (EC 3.1.3.48)	protein	553	36% helix, 23% strand	Q59EE0

Pockets

10 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	152	0.80	0.97	25	empty
2	65	0.60	0.91	21	empty
3	199	0.52	0.77	33	empty
4	151	0.49	0.78	19	empty
5	106	0.42	0.77	21	empty

Compared structures

2NLK · Crystal structure of D1 and D2 catalytic domains of human Protein Tyrosine Phosphatase… · 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 Q59EE0
Elsewhere: RCSB PDB 2NLK · PDBe 2NLK · UniProt Q59EE0

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