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New structure of cold-active protein tyrosine phosphatase at 1.1 ångström

Analyse New structure of cold-active protein tyrosine phosphatase at 1.1 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Z72
Type: protein
Length: 338 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-tyrosine-phosphatase
EC: 3.1.3.48
UniProt: Q9S427
Ligands: ZN
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-tyrosine-phosphatase (EC 3.1.3.48)	protein	338	30% helix, 23% strand	Q9S427

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

4 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	51	0.63	0.94	20	empty
2	79	0.46	0.81	16	empty
3	96	0.45	0.80	24	empty
4	79	0.32	0.74	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2Z72 · New Structure Of Cold-Active Protein Tyrosine Phosphatase At 1.1 Angstrom · the same entry in another collection · chain A against A, TM-score 1.00

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 Q9S427
Elsewhere: RCSB PDB 2Z72 · PDBe 2Z72 · UniProt Q9S427

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