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Structure of rubisco lsmt bound to adomet

Analyse Structure of rubisco lsmt bound to adomet in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H21
Type: protein
Length: 1,305 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q43088

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	425	—	Q43088
B	—	protein	441	—	Q43088
C	—	protein	439	—	Q43088

Compared structures

2H21 · Structure of Rubisco LSMT bound to AdoMet · the same entry in another collection · chain B against B, TM-score 1.00
Q43088 · AlphaFold monomer V2.0 prediction for ribulose-1,5 bisphosphate CARBOXYLASE/OXYGENASE… · 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 Q43088
Elsewhere: RCSB PDB 2H21 · PDBe 2H21 · UniProt Q43088

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