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Crystal structure of the tandem phosphatase domains of rptp lar

Analyse Crystal structure of the tandem phosphatase domains of rptp lar in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LAR
Type: protein
Length: 1,099 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (lar)
EC: 3.1.3.48
UniProt: P10586
Pockets: 18 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (lar) (EC 3.1.3.48)	protein	566	33% helix, 21% strand	P10586
B	Protein (lar) (EC 3.1.3.48)	protein	533	33% helix, 22% strand	P10586

Pockets

18 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	498	0.79	0.86	49	empty
2	481	0.78	0.86	47	empty
3	280	0.59	0.78	28	empty
4	301	0.56	0.76	25	empty
5	174	0.53	0.79	24	empty

Interfaces

1 interface between chains.

A–B · 452 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1LAR · Crystal structure of the tandem phosphatase domains of rptp lar · the same entry in another collection · chain A against A, TM-score 1.00
P10586 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase F… · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P10586
Elsewhere: RCSB PDB 1LAR · PDBe 1LAR · UniProt P10586

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