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Nucleotide-dependent conformational changes in a protease-associated ATPase hslu

Analyse Nucleotide-dependent conformational changes in a protease-associated ATPase hslu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HQY
Type: protein
Length: 1,512 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock locus hslv; Heat shock locus hslu
UniProt: P31059, P0A6H5
Ligands: ADP
Pockets: 13 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Heat shock locus hslv	protein	174	36% helix, 29% strand	P31059
E, F	Heat shock locus hslu	protein	408	55% helix, 10% strand	P0A6H5

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains E, F

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

Pockets

13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1115	0.87	0.88	114	ADP
2	639	0.68	0.77	69	empty
3	504	0.66	0.77	63	empty
4	270	0.58	0.78	35	ADP
5	134	0.45	0.77	20	empty

Interfaces

5 interfaces between chains.

E–F · 2369 Å² buried · 28 hydrogen bonds · protein-protein
A–B · 510 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 453 Å² buried · 6 hydrogen bonds · protein-protein
B–F · 329 Å² buried · 7 hydrogen bonds · protein-protein
A–E · 248 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1HQY · Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU · the same entry in another collection · chain C against C, TM-score 1.00
P0A6H5 · AlphaFold monomer V2.0 prediction for ATP-dependent protease ATPase subunit hslu (P0A6H5) · a predicted model of the same protein · chain E against A, TM-score 0.93

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 P31059
Every structure of UniProt P0A6H5
Elsewhere: RCSB PDB 1HQY · PDBe 1HQY · UniProt P31059 · UniProt P0A6H5

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