Research workbench

V59W mutant of dehaloperoxidase a from amphitrite ornata treated with fluoride

Analyse V59W mutant of dehaloperoxidase a from amphitrite ornata treated with fluoride in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MNH
Type: protein
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dehaloperoxidase a
UniProt: Q9NAV8
Ligands: HEM, SO4
Pockets: 4 · best druggability 0.68

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dehaloperoxidase a	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

4 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	226	0.68	0.84	31	HEM
2	222	0.68	0.84	28	HEM
3	142	0.50	0.79	20	SO4
4	54	0.26	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 362 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7MNH · V59W mutant of Dehaloperoxidase A from Amphitrite ornata treated with Fluoride · 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 7MNH · PDBe 7MNH · UniProt Q9NAV8

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