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Structure of the 14-3-3 / H+-ATPase plant complex

Analyse Structure of the 14-3-3 / H+-ATPase plant complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O98
Type: protein
Length: 573 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P93343, Q40409

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	234	—	P93343
B	—	protein	237	—	P93343
P	—	protein	52	—	Q40409
Q	—	protein	50	—	Q40409

Compared structures

2O98 · Structure of the 14-3-3 / H+-ATPase plant complex · the same entry in another collection · chain A against A, TM-score 1.00
P93343 · AlphaFold monomer V2.0 prediction for 14-3-3-like protein C (P93343) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P93343
Every structure of UniProt Q40409
Elsewhere: RCSB PDB 2O98 · PDBe 2O98 · UniProt P93343 · UniProt Q40409

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