Research workbench

Solution NMR structure of DOT1L in complex with AF9 (DOT1L-AF9)

Analyse Solution NMR structure of DOT1L in complex with AF9 (DOT1L-AF9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MV7
Type: protein
Length: 94 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein af-9; Histone-lysine N-methyltransferase, H3 lysine-79 specific
EC: 2.1.1.43
UniProt: P42568, Q8TEK3

Structure

solution nmr · 2 distinct chains · 47% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein af-9	protein	69	64% helix, 12% strand	P42568
B	Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.43)	protein	25	0% helix, 12% strand	Q8TEK3

Interfaces

1 interface between chains.

A–B · 855 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2MV7 · Solution NMR structure of DOT1L in complex with AF9 (DOT1L-AF9) · the same entry in another collection · chain A against A, TM-score 1.00
P42568 · AlphaFold monomer V2.0 prediction for protein af-9 (P42568) · a predicted model of the same protein · chain A against A, TM-score 0.83
Q8TEK3 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-79… · a predicted model of the same protein · chain B against A, TM-score 0.30

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 P42568
Every structure of UniProt Q8TEK3
Elsewhere: RCSB PDB 2MV7 · PDBe 2MV7 · UniProt P42568 · UniProt Q8TEK3

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