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Crystal structure of the conserved hypothetical protein TT1751 from thermus thermophilus HB8

Analyse Crystal structure of the conserved hypothetical protein TT1751 from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1J3M
Type: protein
Length: 254 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: The conserved hypothetical protein TT1751
UniProt: Q84BQ8
Ligands: SO3
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	The conserved hypothetical protein TT1751	protein	127	55% helix, 26% strand	Q84BQ8

Ligands and binding sites

SO3 · Sulfite ion · ion · chains A

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

Pockets

6 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	112	0.79	0.97	31	empty
2	78	0.75	0.97	19	empty
3	113	0.50	0.80	17	empty
4	60	0.44	0.82	16	empty
5	84	0.42	0.79	14	empty

Interfaces

1 interface between chains.

A–B · 1415 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1J3M · Crystal structure of the conserved hypothetical protein TT1751 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 Q84BQ8
Elsewhere: RCSB PDB 1J3M · PDBe 1J3M · UniProt Q84BQ8

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