Research workbench

Crystal structure of the C-terminal 10 kda subdomain from C. elegans HSP70

Analyse Crystal structure of the C-terminal 10 kda subdomain from C. elegans HSP70 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P32
Type: protein
Length: 492 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock 70 kda protein a
UniProt: P09446
Ligands: SO4
Pockets: 6 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Heat shock 70 kda protein a	protein	82	78% helix, 0% strand	P09446

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, C, F, B, D, E

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

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	105	0.69	0.93	24	empty
2	501	0.64	0.77	41	SO4
3	499	0.64	0.77	38	SO4
4	496	0.64	0.76	41	SO4
5	220	0.56	0.79	22	empty

Interfaces

12 interfaces between chains.

C–D · 483 Å² buried · 7 hydrogen bonds · protein-protein
B–E · 480 Å² buried · 7 hydrogen bonds · protein-protein
A–F · 479 Å² buried · 7 hydrogen bonds · protein-protein
D–F · 380 Å² buried · 3 hydrogen bonds · protein-protein
E–F · 375 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2P32 · Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70 · the same entry in another collection · chain C against C, TM-score 1.00
P09446 · AlphaFold monomer V2.0 prediction for heat shock protein HSP-1 (P09446) · a predicted model of the same protein · chain A against A, TM-score 0.86

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 P09446
Elsewhere: RCSB PDB 2P32 · PDBe 2P32 · UniProt P09446

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.