MolNFT v1 · #25768 · protein

Kinase recruitment domain of the stress phosphatase rsbu

1W53 · Phosphoserine phosphatase rsbu: “Kinase recruitment domain of the stress phosphatase rsbu”. X-ray diffraction, 1 ligand (XE), 1 pocket (best druggability 0.33). MolNFT v1 #25768 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1W53
Type: protein
Length: 84 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoserine phosphatase rsbu
UniProt: P40399
Ligands: XE
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoserine phosphatase rsbu	protein	84	85% helix, 0% strand	P40399

Ligands and binding sites

XE · Xenon · ion · chains A
GOL · Glycerol · additive · 2 copies · 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	55	0.33	0.76	13	empty

Compared structures

1W53 · Kinase recruitment domain of the stress phosphatase RsbU · the same entry in another collection · chain A against A, TM-score 1.00
P40399 · AlphaFold monomer V2.0 prediction for phosphoserine phosphatase rsbu (P40399) · 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 P40399
Elsewhere: RCSB PDB 1W53 · PDBe 1W53 · UniProt P40399

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