MolNFT v1 · #148090 · protein

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

6EWN: “Hspa from thermosynechococcus vulcanus in the presence of 2M urea with initial stages of denaturation”. X-ray diffraction, 1 ligand (URE), 5 pockets (best druggability 0.71). MolNFT v1 #148090 on GenesisL1: 3D structure, binding…

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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