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Prl-1 C104S mutant in complex with sulfate

Analyse Prl-1 C104S mutant in complex with sulfate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZCL
Type: protein
Length: 304 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein tyrosine phosphatase 4A1
EC: 3.1.3.48
UniProt: Q78EG7
Ligands: SO4
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein tyrosine phosphatase 4A1 (EC 3.1.3.48)	protein	152	39% helix, 16% strand	Q78EG7

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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	109	0.50	0.81	29	empty

Interfaces

1 interface between chains.

A–B · 615 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1ZCL · prl-1 c104s mutant in complex with sulfate · the same entry in another collection · chain A against A, TM-score 1.00
Q78EG7 · AlphaFold monomer V2.0 prediction for protein tyrosine phosphatase type iva 1 (Q78EG7) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q78EG7
Elsewhere: RCSB PDB 1ZCL · PDBe 1ZCL · UniProt Q78EG7

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