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The crystal structure of E. COLI fis mutant R71L

Analyse The crystal structure of E. COLI fis mutant R71L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ETO
Type: protein
Length: 181 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Factor for inversion stimulation
UniProt: P0A6R3
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 2 distinct chains · 60% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Factor for inversion stimulation	protein	87	62% helix, 9% strand	P0A6R3
B	Factor for inversion stimulation	protein	94	57% helix, 9% strand	P0A6R3

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	58	0.27	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 2343 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

1ETO · The crystal structure of E. COLI fis mutant R71L · 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 0.94

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 1ETO · PDBe 1ETO · UniProt P0A6R3

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