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Human skeletal calsequestrin, D210G mutant low-calcium complex

Analyse Human skeletal calsequestrin, D210G mutant low-calcium complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CRE
Type: protein
Length: 347 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calsequestrin-1
UniProt: P31415
Ligands: CA
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calsequestrin-1	protein	347	35% helix, 20% strand	P31415

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A

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

Pockets

6 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	80	0.72	0.95	18	empty
2	343	0.69	0.82	39	empty
3	194	0.56	0.79	37	empty
4	86	0.45	0.79	15	MPD
5	64	0.36	0.77	14	empty

Compared structures

5CRE · Human skeletal calsequestrin, D210G mutant low-calcium complex · the same entry in another collection · chain A against A, TM-score 1.00
P31415 · AlphaFold monomer V2.0 prediction for calsequestrin-1 (P31415) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P31415
Elsewhere: RCSB PDB 5CRE · PDBe 5CRE · UniProt P31415

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