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Crystal structure of PYST1 (MKP3)

Analyse Crystal structure of PYST1 (MKP3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MKP
Type: protein
Length: 144 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PYST1
EC: 3.1.3.48, 3.1.3.16
UniProt: Q16828
Ligands: CL
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PYST1 (EC 3.1.3.48, 3.1.3.16)	protein	144	40% helix, 20% strand	Q16828

Ligands and binding sites

CL · Chloride ion · ion · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 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	73	0.49	0.83	14	MPD
2	56	0.28	0.74	13	empty

Compared structures

1MKP · Crystal structure of PYST1 (MKP3) · the same entry in another collection · chain A against A, TM-score 1.00
Q16828 · AlphaFold monomer V2.0 prediction for dual specificity protein phosphatase 6 (Q16828) · a predicted model of the same protein · chain A against A, TM-score 0.86

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 Q16828
Elsewhere: RCSB PDB 1MKP · PDBe 1MKP · UniProt Q16828

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