Research workbench

N-terminal domain of stress-induced protein-1 (sti-1) from C.ELEGANS

Analyse N-terminal domain of stress-induced protein-1 (sti-1) from C.ELEGANS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GCN
Type: protein
Length: 254 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein sti-1
UniProt: O16259
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein sti-1	protein	127	82% helix, 0% strand	O16259

Ligands and binding sites

PGE · Triethylene glycol · additive · chains B

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

Pockets

2 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	223	0.56	0.78	25	empty
2	64	0.28	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 534 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4GCN · N-terminal domain of stress-induced protein-1 (STI-1) from C.elegans · the same entry in another collection · chain A against A, TM-score 1.00
O16259 · AlphaFold monomer V2.0 prediction for stress-induced-phosphoprotein 1 (O16259) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 O16259
Elsewhere: RCSB PDB 4GCN · PDBe 4GCN · UniProt O16259

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