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Thermus thermophilus dnaj

Analyse Thermus thermophilus dnaj in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J80
Type: protein
Length: 1,084 residues
Chains: 4
Method: x-ray diffraction; epr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein dnaj 2
UniProt: Q56237

Structure

x-ray diffraction; epr · 1 distinct chain · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Chaperone protein dnaj 2	protein	271	31% helix, 24% strand	Q56237

Interfaces

3 interfaces between chains.

A–B · 1669 Å² buried · 15 hydrogen bonds · protein-protein
C–D · 1654 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 213 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 24 modified (engineered).

Compared structures

4J80 · Thermus thermophilus DnaJ · the same entry in another collection · chain D against D, TM-score 1.00
Q56237 · AlphaFold monomer V2.0 prediction for chaperone protein dnaj 2 (Q56237) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 Q56237
Elsewhere: RCSB PDB 4J80 · PDBe 4J80 · UniProt Q56237

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