Research workbench

Crystal structure of SEFD_DSCA in H2O

Analyse Crystal structure of SEFD_DSCA in H2O in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UIY
Type: protein
Length: 131 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chimera protein of sefd and sefa
UniProt: Q53997, P12061
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chimera protein of sefd and sefa	protein	131	0% helix, 47% strand	Q53997, P12061

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	176	0.50	0.77	21	empty

Compared structures

3UIY · Crystal structure of SefD_dscA in H2O · the same entry in another collection · chain A against A, TM-score 1.00
P12061 · AlphaFold monomer V2.0 prediction for fimbrial protein (P12061) · a predicted model of the same protein · chain A against A, TM-score 0.68

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 Q53997
Every structure of UniProt P12061
Elsewhere: RCSB PDB 3UIY · PDBe 3UIY · UniProt Q53997 · UniProt P12061

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