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Crystal structure of the conserved protein TT1381 from thermus thermophilus HB8

Analyse Crystal structure of the conserved protein TT1381 from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UDX
Type: protein
Length: 412 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: The GTP-binding protein obg
UniProt: Q7X493
Pockets: 5 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	The GTP-binding protein obg	protein	412	23% helix, 26% strand	Q7X493

Ligands and binding sites

ACT · Acetate ion · additive · 2 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	77	0.51	0.84	12	MPD
2	141	0.48	0.77	19	empty
3	109	0.46	0.79	20	empty
4	60	0.41	0.81	17	empty
5	64	0.27	0.72	15	empty

Compared structures

1UDX · Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8 · 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 Q7X493
Elsewhere: RCSB PDB 1UDX · PDBe 1UDX · UniProt Q7X493

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