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The NMR structure of alpha-parvin CH2/PAXILLIN LD1 complex

Analyse The NMR structure of alpha-parvin CH2/PAXILLIN LD1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2K2R
Type: protein
Length: 139 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-parvin; Paxillin
UniProt: Q9NVD7
Pockets: 1 · best druggability 0.59

Structure

solution nmr · 2 distinct chains · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-parvin	protein	129	64% helix, 0% strand	Q9NVD7
B	Paxillin	protein	10	80% helix, 0% 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	108	0.59	0.85	24	empty

Interfaces

1 interface between chains.

A–B · 392 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2K2R · The NMR structure of alpha-parvin CH2/paxillin LD1 complex · the same entry in another collection · chain A against A, TM-score 1.00
Q9NVD7 · AlphaFold monomer V2.0 prediction for alpha-parvin (Q9NVD7) · 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 Q9NVD7
Elsewhere: RCSB PDB 2K2R · PDBe 2K2R · UniProt Q9NVD7

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