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Structure of snasp core in complex with H3 ALPHA3 helix peptide

Analyse Structure of snasp core in complex with H3 ALPHA3 helix peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V1L
Type: protein
Length: 235 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform 2 of nuclear autoantigenic sperm protein; H3 ALPHA3 helix peptide
UniProt: P84243
Pockets: 3 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Isoform 2 of nuclear autoantigenic sperm protein	protein	221	85% helix, 0% strand	—
V	H3 ALPHA3 helix peptide	protein	14	64% helix, 0% strand	P84243

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	154	0.49	0.78	26	empty
2	55	0.36	0.79	15	empty
3	78	0.35	0.76	19	empty

Interfaces

1 interface between chains.

B–V · 522 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7V1L · Structure of sNASP core in complex with H3 alpha3 helix peptide · the same entry in another collection · chain B against B, TM-score 1.00
P84243 · AlphaFold monomer V2.0 prediction for histone H3.3 (P84243) · a predicted model of the same protein · chain V against A, TM-score 0.57

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 P84243
Elsewhere: RCSB PDB 7V1L · PDBe 7V1L · UniProt P84243

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