MolNFT v1 · #110224 · protein

Crystal structure of hemerythrin: L114A mutant

4XQ1 · Bacteriohemerythrin: “Crystal structure of hemerythrin: L114A mutant”. X-ray diffraction, 3 ligands (FE, NA, NO3), 1 pocket (best druggability 0.72). MolNFT v1 #110224 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4XQ1
Type: protein
Length: 131 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bacteriohemerythrin
UniProt: Q60AX2
Ligands: FE, NA, NO3
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bacteriohemerythrin	protein	131	77% helix, 0% strand	Q60AX2

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A
NA · Sodium ion · metal · chains A
NO3 · Nitrate ion · ion · 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	106	0.72	0.93	25	NO3, NA

Compared structures

4XQ1 · Crystal structure of hemerythrin: L114A mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q60AX2 · AlphaFold monomer V2.0 prediction for bacteriohemerythrin (Q60AX2) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 Q60AX2
Elsewhere: RCSB PDB 4XQ1 · PDBe 4XQ1 · UniProt Q60AX2

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