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Crystal structure of the H-nox domain from nostoc sp. pcc 7120 complexed to no

Analyse Crystal structure of the H-nox domain from nostoc sp. pcc 7120 complexed to no in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O0C
Type: protein
Length: 364 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALR2278 protein
UniProt: Q8YUQ7
Ligands: HEM, NO
Pockets: 2 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ALR2278 protein	protein	182	54% helix, 17% strand	Q8YUQ7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
NO · Nitric oxide · ion · 2 copies · chains A, 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1029	0.89	0.90	110	HEM, NO
2	117	0.47	0.79	33	empty

Interfaces

1 interface between chains.

A–B · 439 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2O0C · Crystal structure of the H-NOX domain from Nostoc sp. PCC 7120 complexed to NO · 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 Q8YUQ7
Elsewhere: RCSB PDB 2O0C · PDBe 2O0C · UniProt Q8YUQ7

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