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Solution structure of the PDZ2 domain from human phosphatase HPTP1E complexed with a peptide

Analyse Solution structure of the PDZ2 domain from human phosphatase HPTP1E complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1D5G
Type: protein
Length: 111 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human phosphatase HPTP1E; Peptide fadseadeneqvsav
UniProt: Q12923
Pockets: 1 · best druggability 0.75

Structure

solution nmr · 2 distinct chains · 14% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Human phosphatase HPTP1E	protein	96	16% helix, 31% strand	Q12923
B	Peptide fadseadeneqvsav	protein	15	0% helix, 7% strand	—

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	252	0.75	0.88	45	empty

Interfaces

1 interface between chains.

A–B · 484 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1D5G · Solution structure of the PDZ2 domain from human phosphatase HPTP1E complexed with a… · the same entry in another collection · chain A against A, TM-score 1.00
Q12923 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 13… · a predicted model of the same protein · chain A against A, TM-score 0.78

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 Q12923
Elsewhere: RCSB PDB 1D5G · PDBe 1D5G · UniProt Q12923

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