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Crystal structure analysis of the human tub protein (isoform a) spanning residues 289 through 561

Analyse Crystal structure analysis of the human tub protein (isoform a) spanning… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1S31
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tubby isoform a
UniProt: P50607
Pockets: 4 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tubby isoform a	protein	273	13% helix, 33% strand	P50607

Ligands and binding sites

PGE · Triethylene glycol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	198	0.53	0.78	34	empty
2	50	0.41	0.82	15	empty
3	67	0.31	0.75	19	empty
4	62	0.31	0.75	15	empty

Compared structures

1S31 · Crystal Structure Analysis of the human Tub protein (isoform a) spanning residues 289… · the same entry in another collection · chain A against A, TM-score 1.00
P50607 · AlphaFold monomer V2.0 prediction for tubby protein homolog (P50607) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P50607
Elsewhere: RCSB PDB 1S31 · PDBe 1S31 · UniProt P50607

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