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NMR structure of the RRM1 domain of HRB1

Analyse NMR structure of the RRM1 domain of HRB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MZR
Type: protein
Length: 95 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein HRB1
UniProt: P38922
Pockets: 1 · best druggability 0.50

Structure

solution nmr · 1 distinct chain · 18% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein HRB1	protein	95	18% helix, 22% strand	P38922

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	56	0.50	0.87	16	empty

Compared structures

2MZR · NMR structure of the RRM1 domain of Hrb1 · the same entry in another collection · chain A against A, TM-score 1.00
P38922 · AlphaFold monomer V2.0 prediction for protein HRB1 (P38922) · a predicted model of the same protein · chain A against A, TM-score 0.72

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 P38922
Elsewhere: RCSB PDB 2MZR · PDBe 2MZR · UniProt P38922

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