MolNFT v1 · #87054 · protein

Structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form

4BPC · Receptor-type tyrosine-protein phosphatase S: “Structure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid form”. X-ray diffraction, 7 pockets (best druggability 0.76). MolNFT v1 #87054 on GenesisL1…

PDB: 4BPC
Type: protein
Length: 567 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor-type tyrosine-protein phosphatase S
EC: 3.1.3.48
UniProt: Q13332
Pockets: 7 · best druggability 0.76

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Receptor-type tyrosine-protein phosphatase S (EC 3.1.3.48)	protein	567	37% helix, 23% strand	Q13332

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	403	0.76	0.86	42	empty
2	223	0.56	0.78	23	empty
3	164	0.48	0.77	21	empty
4	121	0.43	0.77	23	empty
5	113	0.43	0.77	21	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

4BPC · Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic… · the same entry in another collection · chain A against A, TM-score 1.00
Q13332 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase S… · 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 Q13332
Elsewhere: RCSB PDB 4BPC · PDBe 4BPC · UniProt Q13332

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