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Structure of mycobacterium thermoresistibile trehalose-6-phosphate synthase (apo form).

Analyse Structure of mycobacterium thermoresistibile trehalose-6-phosphate synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5JIJ
Type: protein
Length: 461 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA,ALPHA-trehalose-phosphate synthase
UniProt: A0A117IMA6
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA,ALPHA-trehalose-phosphate synthase	protein	461	45% helix, 21% strand	A0A117IMA6

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 9 copies · chains A
NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · chains A

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

Pockets

3 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	1042	0.74	0.76	61	EDO
2	72	0.40	0.79	17	empty
3	86	0.35	0.76	27	EDO

Compared structures

5JIJ · Structure of Mycobacterium thermoresistibile trehalose-6-phosphate synthase (APO form). · 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 A0A117IMA6
Elsewhere: RCSB PDB 5JIJ · PDBe 5JIJ · UniProt A0A117IMA6

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