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Structure of the inositol-1-phosphate CTP transferase from T. maritima.

Analyse Structure of the inositol-1-phosphate CTP transferase from T. maritima. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JD0
Type: protein
Length: 245 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleotidyl transferase
UniProt: G4FFF4
Ligands: 1KH, NA, PO4, CL
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleotidyl transferase	protein	245	33% helix, 28% strand	G4FFF4

Ligands and binding sites

1KH · arsenoribose · ligand · chains A
NA · Sodium ion · metal · 8 copies · chains A
PO4 · Phosphate ion · ion · 3 copies · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	313	0.65	0.81	34	1KH, CL, NA, GOL

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4JD0 · Structure of the inositol-1-phosphate CTP transferase from T. maritima. · 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 G4FFF4
Elsewhere: RCSB PDB 4JD0 · PDBe 4JD0 · UniProt G4FFF4

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