Research workbench

Crystal structure of a putative nuclease with a ribonuclease H-like motif fold (TM1739) from thermotoga maritima at 2.20 a resolution

Analyse Crystal structure of a putative nuclease with a ribonuclease H-like motif fold… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZUP
Type: protein
Length: 580 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein TM1739
UniProt: Q9X261
Pockets: 6 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein TM1739	protein	293	25% helix, 32% strand	Q9X261
B	Hypothetical protein TM1739	protein	287	23% helix, 31% strand	Q9X261

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	679	0.65	0.75	69	empty
2	619	0.65	0.76	53	empty
3	163	0.56	0.81	34	empty
4	107	0.51	0.82	22	empty
5	157	0.48	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 2627 Å² buried · 47 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

1ZUP · Crystal structure of a putative nuclease with a ribonuclease H-like motif fold (TM1739)… · 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 Q9X261
Elsewhere: RCSB PDB 1ZUP · PDBe 1ZUP · UniProt Q9X261

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.