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F78L tt H-nox

Analyse F78L tt H-nox in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FDK
Type: protein
Length: 376 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyl-accepting chemotaxis protein
UniProt: Q8RBX6
Ligands: HEM, OXY
Pockets: 6 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Methyl-accepting chemotaxis protein	protein	188	48% helix, 20% strand	Q8RBX6

Ligands and binding sites

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

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

Pockets

6 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	337	0.84	0.93	39	HEM, OXY
2	524	0.81	0.87	62	HEM, OXY
3	199	0.50	0.76	25	empty
4	92	0.39	0.76	17	empty
5	89	0.39	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 670 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4FDK · F78L Tt H-NOX · 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 Q8RBX6
Elsewhere: RCSB PDB 4FDK · PDBe 4FDK · UniProt Q8RBX6

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