Research workbench

Crystal structure of the macro-domain of human core histone variant MACROH2A1.2

Analyse Crystal structure of the macro-domain of human core histone variant MACROH2A1.2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZR5
Type: protein
Length: 376 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: H2AFY protein
UniProt: O75367
Pockets: 3 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	H2AFY protein	protein	189	42% helix, 20% strand	O75367
B	H2AFY protein	protein	187	41% helix, 21% strand	O75367

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	410	0.61	0.77	43	empty
2	250	0.57	0.78	36	empty
3	69	0.39	0.78	16	empty

Interfaces

1 interface between chains.

A–B · 425 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1ZR5 · Crystal structure of the macro-domain of human core histone variant macroH2A1.2 · the same entry in another collection · chain A against A, TM-score 1.00
O75367 · AlphaFold monomer V2.0 prediction for core histone macro-H2A.1 (O75367) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 O75367
Elsewhere: RCSB PDB 1ZR5 · PDBe 1ZR5 · UniProt O75367

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.