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Crystal structure of aquifex aeolicus RNase H3

Analyse Crystal structure of aquifex aeolicus RNase H3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VN5
Type: protein
Length: 255 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease hiii
EC: 3.1.26.4
UniProt: O67644
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribonuclease hiii (EC 3.1.26.4)	protein	255	46% helix, 19% strand	O67644

Pockets

2 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	163	0.52	0.79	25	empty
2	77	0.34	0.76	18	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

3VN5 · Crystal structure of Aquifex aeolicus RNase H3 · the same entry in another collection · chain A against A, TM-score 1.00
O67644 · AlphaFold monomer V2.0 prediction for ribonuclease hiii (O67644) · a predicted model of the same protein · chain A against A, TM-score 0.72

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 O67644
Elsewhere: RCSB PDB 3VN5 · PDBe 3VN5 · UniProt O67644

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