Research workbench

Crystal structure of human MCPH1 tandem brct domains

Analyse Crystal structure of human MCPH1 tandem brct domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SHT
Type: protein
Length: 561 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microcephalin
UniProt: Q8NEM0
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 37% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Microcephalin	protein	188	36% helix, 16% strand	Q8NEM0
B	Microcephalin	protein	187	37% helix, 17% strand	Q8NEM0
C	Microcephalin	protein	186	39% helix, 15% strand	Q8NEM0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	659	0.68	0.77	50	empty
2	129	0.39	0.74	23	empty
3	148	0.39	0.73	23	empty

Interfaces

2 interfaces between chains.

A–B · 202 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 157 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3SHT · Crystal structure of human MCPH1 tandem BRCT domains · the same entry in another collection · chain A against A, TM-score 1.00
Q8NEM0 · AlphaFold monomer V2.0 prediction for microcephalin (Q8NEM0) · 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 Q8NEM0
Elsewhere: RCSB PDB 3SHT · PDBe 3SHT · UniProt Q8NEM0

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