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Crystal structure of aedes aegypti nibbler exo domain

Analyse Crystal structure of aedes aegypti nibbler exo domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7JW2
Type: protein
Length: 437 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exonuclease mut-7 homolog
EC: 3.1.-.-
UniProt: Q179T2
Pockets: 4 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exonuclease mut-7 homolog (EC 3.1.-.-)	protein	219	42% helix, 14% strand	Q179T2
B	Exonuclease mut-7 homolog (EC 3.1.-.-)	protein	218	43% helix, 14% strand	Q179T2

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	237	0.57	0.78	26	empty
2	252	0.56	0.77	26	empty
3	109	0.41	0.76	21	empty
4	79	0.41	0.79	20	empty

Interfaces

1 interface between chains.

A–B · 688 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7JW2 · Crystal structure of Aedes aegypti Nibbler EXO domain · the same entry in another collection · chain A against A, TM-score 1.00
Q179T2 · AlphaFold monomer V2.0 prediction for exonuclease mut-7 homolog (Q179T2) · a predicted model of the same protein · 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 Q179T2
Elsewhere: RCSB PDB 7JW2 · PDBe 7JW2 · UniProt Q179T2

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