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Crystal structure of human translin

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

PDB: 1J1J
Type: protein
Length: 868 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Translin
UniProt: Q15631
Pockets: 7 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Translin	protein	217	77% helix, 0% strand	Q15631

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	692	0.80	0.85	64	empty
2	467	0.73	0.82	37	empty
3	329	0.66	0.81	40	empty
4	478	0.64	0.77	34	empty
5	59	0.40	0.81	16	empty

Interfaces

5 interfaces between chains.

A–B · 921 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 846 Å² buried · 13 hydrogen bonds · protein-protein
A–D · 793 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 762 Å² buried · 11 hydrogen bonds · protein-protein
B–D · 24 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1J1J · Crystal Structure of human Translin · the same entry in another collection · chain A against A, TM-score 1.00
Q15631 · AlphaFold monomer V2.0 prediction for translin (Q15631) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q15631
Elsewhere: RCSB PDB 1J1J · PDBe 1J1J · UniProt Q15631

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