MolNFT v1 · #96109 · protein

RAT PP5 APO

4JA9 · SERINE/THREONINE-protein phosphatase 5: “RAT PP5 APO”. X-ray diffraction, 1 ligand (MG), 3 pockets (best druggability 0.62). MolNFT v1 #96109 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4JA9
Type: protein
Length: 467 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein phosphatase 5
EC: 3.1.3.16
UniProt: P53042
Ligands: MG
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein phosphatase 5 (EC 3.1.3.16)	protein	467	45% helix, 12% strand	P53042

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	331	0.62	0.79	39	empty
2	115	0.46	0.78	21	empty
3	135	0.43	0.76	20	empty

Compared structures

4JA9 · Rat PP5 apo · the same entry in another collection · chain A against A, TM-score 1.00
P53042 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 5 (P53042) · 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 P53042
Elsewhere: RCSB PDB 4JA9 · PDBe 4JA9 · UniProt P53042

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