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Crystal structure of C. elegans cell-death-related nuclease 5(CRN-5)

Analyse Crystal structure of C. elegans cell-death-related nuclease 5(CRN-5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KRN
Type: protein
Length: 343 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein C14A4.5, confirmed by transcript evidence
EC: 3.1.13.-
UniProt: Q17952
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein C14A4.5, confirmed by transcript evidence (EC 3.1.13.-)	protein	183	23% helix, 12% strand	Q17952
B	Protein C14A4.5, confirmed by transcript evidence (EC 3.1.13.-)	protein	160	26% helix, 10% strand	Q17952

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	731	0.77	0.82	90	empty
2	108	0.73	0.94	26	empty
3	331	0.63	0.79	47	empty
4	103	0.61	0.87	22	empty
5	85	0.60	0.88	20	empty

Interfaces

1 interface between chains.

A–B · 983 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

3KRN · Crystal Structure of C. elegans cell-death-related nuclease 5(CRN-5) · 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 Q17952
Elsewhere: RCSB PDB 3KRN · PDBe 3KRN · UniProt Q17952

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