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Structure of protein tyrosine phosphatase 1B (C2)

Analyse Structure of protein tyrosine phosphatase 1B (C2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CM3
Type: protein
Length: 548 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein phosphatase non-receptor type 1
EC: 3.1.3.48
UniProt: P18031
Ligands: CA
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48)	protein	274	32% helix, 22% strand	P18031

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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	207	0.51	0.76	34	empty
2	133	0.46	0.77	22	empty
3	100	0.39	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 343 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2CM3 · Structure of Protein Tyrosine Phosphatase 1B (C2) · 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 P18031
Elsewhere: RCSB PDB 2CM3 · PDBe 2CM3 · UniProt P18031

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