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Crystal structure of cold-active protein-tyrosine phosphatase of a psychrophile shewanella sp.

Analyse Crystal structure of cold-active protein-tyrosine phosphatase of a psychrophile… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1V73
Type: protein
Length: 331 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Psychrophilic phosphatase I
EC: 3.1.3.48
UniProt: Q9S427
Ligands: CA
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Psychrophilic phosphatase I (EC 3.1.3.48)	protein	331	31% helix, 22% strand	Q9S427

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
ACY · Acetic acid · additive · 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	53	0.61	0.93	19	empty
2	84	0.45	0.80	16	empty
3	55	0.39	0.81	17	empty
4	78	0.33	0.75	20	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1V73 · Crystal Structure of Cold-Active Protein-Tyrosine Phosphatase of a Psychrophile… · 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 1V73 · PDBe 1V73 · UniProt Q9S427

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