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Crystal structure of a putative nucleotidyltransferase (TM1012) from thermotoga maritima at 1.87 a resolution

Analyse Crystal structure of a putative nucleotidyltransferase (TM1012) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HX0
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative nucleotidyltransferase TM1012
UniProt: Q9X0A5
Ligands: NA
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative nucleotidyltransferase TM1012	protein	161	41% helix, 33% strand	Q9X0A5

Ligands and binding sites

NA · Sodium ion · metal · 3 copies · chains A
BU1 · 1,4-butanediol · additive · 12 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 5 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	235	0.56	0.78	31	MPD

Compared structures

4HX0 · Crystal structure of a putative nucleotidyltransferase (TM1012) from Thermotoga maritima… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9X0A5
Elsewhere: RCSB PDB 4HX0 · PDBe 4HX0 · UniProt Q9X0A5

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