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Crystal structure of the heptp catalytic domain C270S mutant

Analyse Crystal structure of the heptp catalytic domain C270S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2HVL
Type: protein
Length: 285 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein phosphatase non-receptor type 7
EC: 3.1.3.48
UniProt: P35236
Ligands: PO4
Pockets: 2 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein phosphatase non-receptor type 7 (EC 3.1.3.48)	protein	285	37% helix, 23% strand	P35236

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

2 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	179	0.47	0.76	27	empty
2	72	0.37	0.78	17	empty

Compared structures

2HVL · Crystal structure of the HePTP catalytic domain C270S mutant · the same entry in another collection · chain A against A, TM-score 1.00
P35236 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 7… · a predicted model of the same protein · chain A 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 P35236
Elsewhere: RCSB PDB 2HVL · PDBe 2HVL · UniProt P35236

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