MolNFT v1 · #53059 · protein

Crystal structure of the tyrosine phosphatase CPS4B from steptococcus pneumoniae TIGR4.

2WJE · Tyrosine-protein phosphatase cpsb: “Crystal structure of the tyrosine phosphatase CPS4B from steptococcus pneumoniae TIGR4.”. X-ray diffraction, 1 ligand (MN), 2 pockets (best druggability 0.45). MolNFT v1 #53059 on GenesisL1: 3D…

PDB: 2WJE
Type: protein
Length: 244 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein phosphatase cpsb
EC: 3.1.3.48
UniProt: Q9AHD4
Ligands: MN
Pockets: 2 · best druggability 0.45

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein phosphatase cpsb (EC 3.1.3.48)	protein	244	46% helix, 15% strand	Q9AHD4

Ligands and binding sites

MN · Manganese (II) ion · metal · 3 copies · 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	129	0.45	0.77	19	empty
2	65	0.40	0.80	16	empty

Compared structures

2WJE · Crystal structure of the tyrosine phosphatase Cps4B from Steptococcus pneumoniae TIGR4. · the same entry in another collection · chain A against A, TM-score 1.00
Q9AHD4 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase cpsb (Q9AHD4) · 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 Q9AHD4
Elsewhere: RCSB PDB 2WJE · PDBe 2WJE · UniProt Q9AHD4

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