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Calcium saturated form of human C85M S100A1 mutant

Analyse Calcium saturated form of human C85M S100A1 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2LUX
Type: protein
Length: 186 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein S100-A1
UniProt: P23297
Ligands: CA
Pockets: 5 · best druggability 0.72

Structure

solution nmr · 1 distinct chain · 75% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein S100-A1	protein	93	75% helix, 2% strand	P23297

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.72	0.98	16	empty
2	226	0.57	0.79	28	empty
3	211	0.57	0.79	27	empty
4	50	0.28	0.75	8	empty
5	64	0.28	0.72	10	empty

Interfaces

1 interface between chains.

A–B · 1231 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

2LUX · Calcium saturated form of human C85M S100A1 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 0.75

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 2LUX · PDBe 2LUX · UniProt P23297

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