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Sfx structure of dehaloperoxidase B in the oxyferrous form

Analyse Sfx structure of dehaloperoxidase B in the oxyferrous form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ADX
Type: protein
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dehaloperoxidase B
UniProt: Q9NAV7
Ligands: HEM, SO4, OXY
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dehaloperoxidase B	protein	137	74% helix, 1% strand	Q9NAV7

Ligands and binding sites

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

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

Pockets

2 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	187	0.68	0.86	22	HEM, OXY
2	186	0.64	0.83	25	HEM

Interfaces

1 interface between chains.

A–B · 486 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

7ADX · SFX structure of dehaloperoxidase B in the oxyferrous form · 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 Q9NAV7
Elsewhere: RCSB PDB 7ADX · PDBe 7ADX · UniProt Q9NAV7

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