Research workbench

Crystal structure of the hr-1 domain of human caprin-1 in the P3121 space group

Analyse Crystal structure of the hr-1 domain of human caprin-1 in the P3121 space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4WBP
Type: protein
Length: 239 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Caprin-1
UniProt: Q14444
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 67% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Caprin-1	protein	120	67% helix, 3% strand	Q14444
B	Caprin-1	protein	119	66% helix, 3% strand	Q14444

Pockets

4 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	270	0.61	0.79	32	empty
2	94	0.46	0.80	23	empty
3	103	0.35	0.73	15	empty
4	50	0.29	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 1698 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

4WBP · Crystal structure of the HR-1 domain of human caprin-1 in the P3121 space group · the same entry in another collection · chain A against A, TM-score 1.00
Q14444 · AlphaFold monomer V2.0 prediction for caprin-1 (Q14444) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q14444
Elsewhere: RCSB PDB 4WBP · PDBe 4WBP · UniProt Q14444

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