MolNFT v1 · #108595 · protein

Crystal structure of the exonuclease domain of qip (qde-2 interacting protein) solved by native-sad phasing.

4WBQ · Qde-2-interacting protein: “Crystal structure of the exonuclease domain of qip (qde-2 interacting protein) solved by native-sad phasing.”. X-ray diffraction, 1 ligand (CA), 4 pockets (best druggability 0.57). MolNFT v1 #108595 on…

PDB: 4WBQ
Type: protein
Length: 347 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Qde-2-interacting protein
UniProt: A5JQJ3
Ligands: CA
Pockets: 4 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Qde-2-interacting protein	protein	174	48% helix, 26% strand	A5JQJ3
B	Qde-2-interacting protein	protein	173	46% helix, 28% strand	A5JQJ3

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	80	0.57	0.87	26	empty
2	202	0.49	0.76	30	CA
3	77	0.34	0.76	17	CA
4	55	0.28	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 2874 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4WBQ · Crystal structure of the exonuclease domain of QIP (QDE-2 interacting protein) solved by… · 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 A5JQJ3
Elsewhere: RCSB PDB 4WBQ · PDBe 4WBQ · UniProt A5JQJ3

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