Research workbench

The crystal structure and amino acid sequence of dehaloperoxidase from amphitrite ornata indicate common ancestry with globins

Analyse The crystal structure and amino acid sequence of dehaloperoxidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EW6
Type: protein
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dehaloperoxidase
UniProt: Q9NAV8
Ligands: HEM, SO4
Pockets: 3 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dehaloperoxidase	protein	137	77% helix, 1% strand	Q9NAV8

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	286	0.71	0.84	28	HEM
2	291	0.70	0.83	28	HEM
3	160	0.45	0.75	28	empty

Interfaces

1 interface between chains.

A–B · 257 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1EW6 · The crystal structure and amino acid sequence of dehaloperoxidase from amphitrite ornata… · the same entry in another collection · 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 Q9NAV8
Elsewhere: RCSB PDB 1EW6 · PDBe 1EW6 · UniProt Q9NAV8

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