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Crystal structure of obelin following CA2+ triggered bioluminescence suggests neutral coelenteramide as the primary excited state

Analyse Crystal structure of obelin following CA2+ triggered bioluminescence suggests… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F8P
Type: protein
Length: 190 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Obelin
UniProt: Q27709
Ligands: CEI, CA
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Obelin	protein	190	63% helix, 2% strand	Q27709

Ligands and binding sites

CEI · N-[3-benzyl-5-(4-hydroxyphenyl)pyrazin-2-yl]-2-(4-hydroxyphenyl)acetamide · ligand · chains A
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	319	0.75	0.86	38	CEI

Compared structures

2F8P · Crystal structure of obelin following Ca2+ triggered bioluminescence suggests neutral… · the same entry in another collection · chain A against A, TM-score 1.00
Q27709 · AlphaFold monomer V2.0 prediction for obelin (Q27709) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q27709
Elsewhere: RCSB PDB 2F8P · PDBe 2F8P · UniProt Q27709

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