Research workbench

Clpb NBD2 K601Q from T. thermophilus in complex with mant-dadp

Analyse Clpb NBD2 K601Q from T. thermophilus in complex with mant-dadp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LJ7
Type: protein
Length: 901 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9RA63

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	305	—	Q9RA63
B	—	protein	301	—	Q9RA63
C	—	protein	295	—	Q9RA63

Compared structures

4LJ7 · ClpB NBD2 K601Q from T. thermophilus in complex with MANT-dADP · 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 C against A, TM-score 0.95

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 4LJ7 · PDBe 4LJ7 · UniProt Q9RA63

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