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Structure of the calcineurin-nfat complex

Analyse Structure of the calcineurin-nfat complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JOG
Type: protein
Length: 343 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin-dependent calcineurin a subunit alpha isoform; Nfat
EC: 3.1.3.16
UniProt: Q08209
Pockets: 3 · best druggability 0.56

Structure

solution nmr · 2 distinct chains · 32% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin-dependent calcineurin a subunit alpha isoform (EC 3.1.3.16)	protein	327	33% helix, 19% strand	Q08209
B	Nfat	protein	16	0% helix, 25% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	112	0.56	0.84	20	empty
2	147	0.47	0.77	29	empty
3	64	0.31	0.75	22	empty

Interfaces

1 interface between chains.

A–B · 675 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2JOG · Structure of the calcineurin-NFAT complex · the same entry in another collection · chain A against A, TM-score 1.00
Q08209 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 2B catalytic… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q08209
Elsewhere: RCSB PDB 2JOG · PDBe 2JOG · UniProt Q08209

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