Research workbench

Post-translational S-nitrosylation is an endogenous factor fine-tuning human S100A1 protein properties

Analyse Post-translational S-nitrosylation is an endogenous factor fine-tuning human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LLT
Type: protein
Length: 186 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein S100-A1
UniProt: P23297
Pockets: 2 · best druggability 0.42

Structure

solution nmr · 1 distinct chain · 69% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein S100-A1	protein	93	69% helix, 6% strand	P23297

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.42	0.80	15	empty
2	54	0.33	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 1415 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

2LLT · Post-translational S-nitrosylation is an endogenous factor fine-tuning human S100A1… · the same entry in another collection · chain A against A, TM-score 1.00
P23297 · AlphaFold monomer V2.0 prediction for protein S100-A1 (P23297) · a predicted model of the same protein · chain A against A, TM-score 0.64

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 P23297
Elsewhere: RCSB PDB 2LLT · PDBe 2LLT · UniProt P23297

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