MolNFT v1 · #43591 · protein

Chemical shift assignments and solution structure of human apo-S100A1 E32Q mutant

2LHL · Protein S100-A1: “Chemical shift assignments and solution structure of human apo-S100A1 E32Q mutant”. Solution nmr, 4 pockets (best druggability 0.61). MolNFT v1 #43591 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2LHL
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: 4 · best druggability 0.61

Structure

solution nmr · 1 distinct chain · 63% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein S100-A1	protein	93	63% helix, 4% strand	P23297

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	266	0.61	0.79	31	empty
2	274	0.60	0.78	29	empty
3	110	0.55	0.83	19	empty
4	107	0.55	0.83	21	empty

Interfaces

1 interface between chains.

A–B · 1370 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2LHL · Chemical Shift Assignments and solution structure of human apo-S100A1 E32Q mutant · 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 0.62

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 2LHL · PDBe 2LHL · UniProt P23297

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