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Crystal Structure of Hypothetical protein(TTHA0061) from Thermus thermophilus

Analyse Crystal Structure of Hypothetical protein(TTHA0061) from Thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EI5
Type: protein
Length: 212 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.88
Source: Thermus thermophilus
Molecule: Hypothetical protein TTHA0061
UniProt: Q5SM82
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · resolution 1.88 · 1 distinct chain · 28% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein TTHA0061	protein	106	28% helix, 39% strand	Q5SM82

Ligands and binding sites

BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains B

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

Pockets

3 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	80	0.59	0.88	20	empty
2	161	0.53	0.80	30	empty
3	61	0.41	0.81	22	empty

Interfaces

1 interface between chains.

A–B · 1480 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2EI5 · Crystal structure of hypothetical PROTEIN(TTHA0061) from thermus thermophilus · 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 Q5SM82
Elsewhere: RCSB PDB 2EI5 · PDBe 2EI5 · UniProt Q5SM82

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