Research workbench

Crystal structure of the ferrous bjfixl heme domain

Analyse Crystal structure of the ferrous bjfixl heme domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LSW
Type: protein
Length: 117 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sensor protein fixl
EC: 2.7.3.-
UniProt: P23222
Ligands: HEM
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sensor protein fixl (EC 2.7.3.-)	protein	117	36% helix, 35% strand	P23222

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	258	0.76	0.89	31	HEM

Compared structures

1LSW · Crystal structure of the ferrous BjFixL heme domain · the same entry in another collection · chain A against A, TM-score 1.00
P23222 · AlphaFold monomer V2.0 prediction for sensor protein fixl (P23222) · 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 P23222
Elsewhere: RCSB PDB 1LSW · PDBe 1LSW · UniProt P23222

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.