Research workbench

K97A mutant of E9 DNase domain in complex with IM9

Analyse K97A mutant of E9 DNase domain in complex with IM9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VLO
Type: protein
Length: 222 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Colicin-E9 immunity protein; Colicin E9
UniProt: P13479, P09883
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Colicin-E9 immunity protein	protein	90	54% helix, 2% strand	P13479
B	Colicin E9	protein	132	45% helix, 17% strand	P09883

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 809 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2VLO · K97A mutant of E9 DNase domain in complex with Im9 · the same entry in another collection · chain A against A, TM-score 1.00
P09883 · AlphaFold monomer V2.0 prediction for colicin-E9 (P09883) · a predicted model of the same protein · chain B against A, TM-score 0.97
P13479 · AlphaFold monomer V2.0 prediction for colicin-E9 immunity protein (P13479) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P13479
Every structure of UniProt P09883
Elsewhere: RCSB PDB 2VLO · PDBe 2VLO · UniProt P13479 · UniProt P09883

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