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Hspa from thermosynechococcus vulcanus in the presence of 2M urea with initial stages of denaturation

Analyse Hspa from thermosynechococcus vulcanus in the presence of 2M urea with initial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EWN
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hspa
UniProt: O82825
Ligands: URE
Pockets: 5 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hspa	protein	99	4% helix, 24% strand	O82825

Ligands and binding sites

URE · Urea · ligand · 44 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.71	0.94	21	empty
2	116	0.62	0.87	25	empty
3	97	0.48	0.81	19	empty
4	77	0.42	0.79	20	empty
5	77	0.37	0.77	17	URE

Interfaces

1 interface between chains.

A–B · 212 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

6EWN · HspA from Thermosynechococcus vulcanus in the presence of 2M urea with initial stages of… · the same entry in another collection · chain A against A, TM-score 1.00

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 O82825
Elsewhere: RCSB PDB 6EWN · PDBe 6EWN · UniProt O82825

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