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Refined NMR structure of the FHA1 domain of yeast RAD53

Analyse Refined NMR structure of the FHA1 domain of yeast RAD53 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1J4O
Type: protein
Length: 151 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein kinase SPK1
EC: 2.7.1.-
UniProt: P22216
Pockets: 1 · best druggability 0.35

Structure

solution nmr · 1 distinct chain · 16% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein kinase SPK1 (EC 2.7.1.-)	protein	151	16% helix, 31% strand	P22216

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	52	0.35	0.78	12	empty

Compared structures

1J4O · Refined NMR structure of the FHA1 domain of yeast RAD53 · the same entry in another collection · chain A against A, TM-score 1.00
P22216 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RAD53 (P22216) · a predicted model of the same protein · chain A against A, TM-score 0.83

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 P22216
Elsewhere: RCSB PDB 1J4O · PDBe 1J4O · UniProt P22216

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