MolNFT v1 · #156121 · protein

Induced DNA bending by unique dimerization of higa antitoxin

6LTZ · Putative antitoxin HIGA3: “Induced DNA bending by unique dimerization of higa antitoxin”. X-ray diffraction. MolNFT v1 #156121 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6LTZ
Type: protein
Length: 154 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative antitoxin HIGA3
UniProt: O53333

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative antitoxin HIGA3	protein	78	47% helix, 21% strand	O53333
B	Putative antitoxin HIGA3	protein	76	49% helix, 22% strand	O53333

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains B
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B

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

Interfaces

1 interface between chains.

A–B · 1624 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

6LTZ · Induced DNA bending by unique dimerization of HigA antitoxin · the same entry in another collection · chain A against A, TM-score 1.00
O53333 · AlphaFold monomer V2.0 prediction for putative antitoxin HIGA3 (O53333) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 O53333
Elsewhere: RCSB PDB 6LTZ · PDBe 6LTZ · UniProt O53333

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