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Crystal structure of endonuclease IV (BA4508) from bacillus anthracis at 2.57A resolution.

Analyse Crystal structure of endonuclease IV (BA4508) from bacillus anthracis at 2.57A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XP3
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endonuclease IV
EC: 3.1.21.2
UniProt: Q81LV1
Ligands: ZN, SO4
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endonuclease IV (EC 3.1.21.2)	protein	297	41% helix, 15% strand	Q81LV1

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	127	0.39	0.74	20	ZN, SO4

Compared structures

1XP3 · Crystal Structure of Endonuclease IV (BA4508) from Bacillus anthracis at 2.57A Resolution. · the same entry in another collection · chain A against A, TM-score 1.00
Q81LV1 · AlphaFold monomer V2.0 prediction for probable endonuclease 4 (Q81LV1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q81LV1
Elsewhere: RCSB PDB 1XP3 · PDBe 1XP3 · UniProt Q81LV1

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