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Clpb NBD2 R621Q from T. thermophilus in complex with amppcp

Analyse Clpb NBD2 R621Q from T. thermophilus in complex with amppcp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LJ9
Type: protein
Length: 332 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9RA63

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	332	—	Q9RA63

Compared structures

4LJ9 · ClpB NBD2 R621Q from T. thermophilus in complex with AMPPCP · the same entry in another collection · chain A against A, TM-score 1.00
Q9RA63 · AlphaFold monomer V2.0 prediction for chaperone protein clpb (Q9RA63) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 Q9RA63
Elsewhere: RCSB PDB 4LJ9 · PDBe 4LJ9 · UniProt Q9RA63

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