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Solution structure of the ww domain of hypb

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

PDB: 2MDC
Type: protein
Length: 48 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone-lysine N-methyltransferase SETD2
EC: 2.1.1.43
UniProt: Q9BYW2
Pockets: 1 · best druggability 0.41

Structure

solution nmr · 1 distinct chain · 0% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43)	protein	48	0% helix, 25% strand	Q9BYW2

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	70	0.41	0.80	17	empty

Compared structures

2MDC · Solution structure of the WW domain of HYPB · the same entry in another collection · chain A against A, TM-score 1.00
Q9BYW2 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD2 (Q9BYW2) · a predicted model of the same protein · chain A against A, TM-score 0.36

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 Q9BYW2
Elsewhere: RCSB PDB 2MDC · PDBe 2MDC · UniProt Q9BYW2

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