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The crystal structure of E. COLI fis mutant Q68A

Analyse The crystal structure of E. COLI fis mutant Q68A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ETK
Type: protein
Length: 154 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Factor for inversion stimulation
UniProt: P0A6R3

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Factor for inversion stimulation	protein	75	69% helix, 3% strand	P0A6R3
B	Factor for inversion stimulation	protein	79	66% helix, 3% strand	P0A6R3

Interfaces

1 interface between chains.

A–B · 2160 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

1ETK · The crystal structure of E. COLI fis mutant Q68A · the same entry in another collection · chain A against A, TM-score 1.00
P0A6R3 · AlphaFold monomer V2.0 prediction for DNA-binding protein fis (P0A6R3) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P0A6R3
Elsewhere: RCSB PDB 1ETK · PDBe 1ETK · UniProt P0A6R3

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