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Crystal structure of E. COLI rece exonuclease

Analyse Crystal structure of E. COLI rece exonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3H4R
Type: protein
Length: 219 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exodeoxyribonuclease 8
EC: 3.1.11.-
UniProt: P15032
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exodeoxyribonuclease 8 (EC 3.1.11.-)	protein	219	44% helix, 16% strand	P15032

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	81	0.30	0.73	17	empty

Compared structures

3H4R · Crystal structure of E. coli RecE exonuclease · the same entry in another collection · chain A against A, TM-score 1.00
P15032 · AlphaFold monomer V2.0 prediction for exodeoxyribonuclease 8 (P15032) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P15032
Elsewhere: RCSB PDB 3H4R · PDBe 3H4R · UniProt P15032

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