Research workbench

Apical domain of chloroplast chaperonin 60A

Analyse Apical domain of chloroplast chaperonin 60A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CDJ
Type: protein
Length: 365 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rubisco large subunit-binding protein subunit alpha, chloroplastic
UniProt: Q42694
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rubisco large subunit-binding protein subunit alpha, chloroplastic	protein	182	45% helix, 25% strand	Q42694
B	Rubisco large subunit-binding protein subunit alpha, chloroplastic	protein	183	47% helix, 25% strand	Q42694

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	336	0.62	0.78	43	empty
2	245	0.56	0.78	36	empty
3	135	0.49	0.79	22	empty

Interfaces

1 interface between chains.

A–B · 325 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5CDJ · apical domain of chloroplast chaperonin 60a · the same entry in another collection · chain A against A, TM-score 1.00
Q42694 · AlphaFold monomer V2.0 prediction for rubisco large subunit-binding protein subunit… · 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 Q42694
Elsewhere: RCSB PDB 5CDJ · PDBe 5CDJ · UniProt Q42694

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.