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Crystal structure of an H-nox protein from S. oneidensis in the FE(II)NO ligation state

Analyse Crystal structure of an H-nox protein from S. oneidensis in the FE(II)NO… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4U9B
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: No-binding heme-dependent sensor protein
UniProt: Q8EF49
Ligands: HEM, ZN, NO, PO4
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	No-binding heme-dependent sensor protein	protein	180	55% helix, 17% strand	Q8EF49

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
ZN · Zinc ion · metal · chains A
NO · Nitric oxide · ion · chains A
PO4 · Phosphate ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	449	0.86	0.93	48	HEM, NO
2	70	0.44	0.81	18	empty

Compared structures

4U9B · Crystal structure of an H-NOX protein from S. oneidensis in the Fe(II)NO ligation state · 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 Q8EF49
Elsewhere: RCSB PDB 4U9B · PDBe 4U9B · UniProt Q8EF49

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