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Solution NMR structure of the second and third kh domains of ksrp

Analyse Solution NMR structure of the second and third kh domains of ksrp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JVZ
Type: protein
Length: 164 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Far upstream element-binding protein 2
UniProt: Q92945
Pockets: 1 · best druggability 0.34

Structure

solution nmr · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Far upstream element-binding protein 2	protein	164	36% helix, 20% strand	Q92945

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	85	0.34	0.74	28	empty

Compared structures

2JVZ · Solution NMR Structure of the Second and Third KH Domains of KSRP · the same entry in another collection · chain A against A, TM-score 1.00
Q92945 · AlphaFold monomer V2.0 prediction for far upstream element-binding protein 2 (Q92945) · a predicted model of the same protein · chain A against A, TM-score 0.54

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 Q92945
Elsewhere: RCSB PDB 2JVZ · PDBe 2JVZ · UniProt Q92945

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