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Crystal structure of the small subunit-like domain of rubisco activase from nostoc sp. (strain pcc 7120)

Analyse Crystal structure of the small subunit-like domain of rubisco activase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HAS
Type
protein
Length
174 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribulose bisphosphate CARBOXYLASE/OXYGENASE activase
UniProt
P58555
Ligands
NI
Pockets
1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BRibulose bisphosphate CARBOXYLASE/OXYGENASE activaseprotein8734% helix, 37% strandP58555

Ligands and binding sites

  • NI · Nickel (II) ion · metal · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1820.520.8517empty

Interfaces

1 interface between chains.

  • A–B · 315 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 6HAS · Crystal Structure of the small subunit-like domain of Rubisco activase from Nostoc sp.… · the same entry in another collection · chain A against A, TM-score 1.00
  • P58555 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate CARBOXYLASE/OXYGENASE… · a predicted model of the same protein · chain A against A, TM-score 0.96

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