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Complex structure of C-terminal cftr peptide and extended PDZ2 domain from NHERF1

Analyse Complex structure of C-terminal cftr peptide and extended PDZ2 domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2M0V
Type: protein
Length: 133 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NA(+)/H(+) exchange regulatory cofactor nhe-RF1; C-terminal cftr peptide
UniProt: O14745
Pockets: 1 · best druggability 0.41

Structure

solution nmr · 2 distinct chains · 20% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NA(+)/H(+) exchange regulatory cofactor nhe-RF1	protein	128	21% helix, 23% strand	O14745
B	C-terminal cftr peptide	protein	5	0% helix, 40% strand	—

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.41	0.76	18	empty

Interfaces

1 interface between chains.

A–B · 445 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

2M0V · Complex structure of C-terminal CFTR peptide and extended PDZ2 domain from NHERF1 · the same entry in another collection · chain A against A, TM-score 1.00
O14745 · AlphaFold monomer V2.0 prediction for NA(+)/H(+) exchange regulatory cofactor nhe-RF1… · a predicted model of the same protein · chain A against A, TM-score 0.81

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 O14745
Elsewhere: RCSB PDB 2M0V · PDBe 2M0V · UniProt O14745

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