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Conformational closure of the catalytic site of human CD38 induced by calcium

Analyse Conformational closure of the catalytic site of human CD38 induced by calcium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3F6Y
Type: protein
Length: 235 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ADP-ribosyl cyclase 1
EC: 3.2.2.5
UniProt: P28907
Ligands: CA
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ADP-ribosyl cyclase 1 (EC 3.2.2.5)	protein	235	42% helix, 13% strand	P28907

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	344	0.65	0.80	48	CA

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

3F6Y · Conformational Closure of the Catalytic Site of Human CD38 Induced by Calcium · the same entry in another collection · chain A against A, TM-score 1.00
P28907 · AlphaFold monomer V2.0 prediction for ADP-ribosyl CYCLASE/CYCLIC ADP- ribose hydrolase 1… · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P28907
Elsewhere: RCSB PDB 3F6Y · PDBe 3F6Y · UniProt P28907

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