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Crystal structure of protein tyrosine phosphatase from entamoeba histolytica with hepes in the active site. high resolution, alternative crystal form with 1 molecule in asymmetric unit

Analyse Crystal structure of protein tyrosine phosphatase from entamoeba histolytica… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JS5
Type: protein
Length: 156 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein tyrosine phosphatase
UniProt: C4LSE7
Ligands: NA
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein tyrosine phosphatase	protein	156	46% helix, 15% strand	C4LSE7

Ligands and binding sites

NA · Sodium ion · metal · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.39	0.80	14	EPE

Compared structures

3JS5 · Crystal structure of protein tyrosine phosphatase from Entamoeba histolytica with Hepes… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt C4LSE7
Elsewhere: RCSB PDB 3JS5 · PDBe 3JS5 · UniProt C4LSE7

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