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Crystal sturcture of sedl at 2.4 ångströms resolution

Analyse Crystal sturcture of sedl at 2.4 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H3Q
Type: protein
Length: 140 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sedlin
UniProt: Q9CQP2
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sedlin	protein	140	34% helix, 25% strand	Q9CQP2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.34	0.77	15	empty

Compared structures

1H3Q · Crystal structure of SEDL at 2.4 Angstroms resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q9CQP2 · AlphaFold monomer V2.0 prediction for trafficking protein particle complex subunit 2… · a predicted model of the same protein · chain A against A, TM-score 0.91

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 Q9CQP2
Elsewhere: RCSB PDB 1H3Q · PDBe 1H3Q · UniProt Q9CQP2

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