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Crystal structure of a rubisco-like protein from chlorobium tepidum

Analyse Crystal structure of a rubisco-like protein from chlorobium tepidum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TEL
Type
protein
Length
852 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribulose bisphosphate carboxylase, large subunit
UniProt
Q8KBL4
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibulose bisphosphate carboxylase, large subunitprotein42443% helix, 19% strandQ8KBL4
BRibulose bisphosphate carboxylase, large subunitprotein42842% helix, 19% strandQ8KBL4

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1800.770.9924empty
24930.700.8045empty
33690.690.8242empty
41790.650.8538empty
51820.620.8339empty

Interfaces

1 interface between chains.

  • A–B · 3612 Ų buried · 40 hydrogen bonds · protein-protein

Compared structures

  • 1TEL · Crystal structure of a RubisCO-like protein from Chlorobium tepidum · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8KBL4 · AlphaFold monomer V2.0 prediction for ribulose bisphosphate carboxylase-like protein… · a predicted model of the same protein · chain B against A, TM-score 1.00

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