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Crystal structure of human trnahis guanylyltransferase (THG1)- native I

Analyse Crystal structure of human trnahis guanylyltransferase (THG1)- native I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OTE
Type: protein
Length: 480 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA(HIS) guanylyltransferase
EC: 2.7.7.-
UniProt: Q9NWX6
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	TRNA(HIS) guanylyltransferase (EC 2.7.7.-)	protein	240	50% helix, 17% strand	Q9NWX6

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.64	0.83	34	empty
2	201	0.61	0.82	29	empty
3	225	0.55	0.78	37	empty
4	84	0.32	0.73	11	empty

Interfaces

1 interface between chains.

A–B · 2096 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

3OTE · Crystal structure of human tRNAHis guanylyltransferase (Thg1)- Native I · the same entry in another collection · chain A against A, TM-score 1.00
Q9NWX6 · AlphaFold monomer V2.0 prediction for probable TRNA(HIS) guanylyltransferase (Q9NWX6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9NWX6
Elsewhere: RCSB PDB 3OTE · PDBe 3OTE · UniProt Q9NWX6

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