MolNFT v2 · #152721 · protein

Structure of Thermus thermophilus ClpP in complex with bortezomib

6HWM: “Structure of Thermus thermophilus ClpP in complex with bortezomib”. X-ray diffraction at 2.7, 1 ligand (BO2). MolNFT v2 #152721 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HWM
Type: protein
Length: 1,311 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.7
Source: Thermus thermophilus
UniProt: Q5SKM8
Ligands: BO2

Structure

x-ray diffraction · resolution 2.7 · 7 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	185	—	Q5SKM8
B	—	protein	192	—	Q5SKM8
C	—	protein	183	—	Q5SKM8
D	—	protein	184	—	Q5SKM8
E	—	protein	195	—	Q5SKM8
F	—	protein	189	—	Q5SKM8
G	—	protein	183	—	Q5SKM8

Ligands and binding sites

BO2 · N-[(1R)-1-(dihydroxyboryl)-3-methylbutyl]-N-(pyrazin-2-ylcarbonyl)-L-phenylalaninamide · ligand · 7 copies · chains A, B, C, D, E, F, G
PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains C, E, G

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6HWM · Structure of thermus thermophilus clpp in complex with bortezomib · the same entry in another collection · chain G against G, TM-score 1.00
Q5SKM8 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease proteolytic subunit… · a predicted model of the same protein · chain G 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 Q5SKM8
Elsewhere: RCSB PDB 6HWM · PDBe 6HWM · UniProt Q5SKM8

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