Research workbench

The crystal structure of MLL2 in complex with ASH2L and RBBP5

Analyse The crystal structure of MLL2 in complex with ASH2L and RBBP5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BRE
Type: protein
Length: 725 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9UBL3, Q9UMN6, Q15291
Ligands: ZN

Structure

x-ray diffraction · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	179	—	Q9UBL3
B	—	protein	164	—	Q9UMN6
E	—	protein	164	—	Q9UMN6
D	—	protein	179	—	Q9UBL3
C	—	protein	20	—	Q15291
F	—	protein	19	—	Q15291

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains B, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7BRE · The crystal structure of MLL2 in complex with ASH2L and RBBP5 · the same entry in another collection · chain A against A, TM-score 1.00
Q9UBL3 · AlphaFold monomer V2.0 prediction for SET1/ASH2 histone methyltransferase complex subunit… · a predicted model of the same protein · chain A against A, TM-score 0.98
Q15291 · AlphaFold monomer V2.0 prediction for retinoblastoma-binding protein 5 (Q15291) · a predicted model of the same protein · chain C against A, TM-score 0.43

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 Q9UBL3
Every structure of UniProt Q9UMN6
Every structure of UniProt Q15291
Elsewhere: RCSB PDB 7BRE · PDBe 7BRE · UniProt Q9UBL3 · UniProt Q9UMN6 · UniProt Q15291

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