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Apo nis synthetase desd variant R306Q

Analyse Apo nis synthetase desd variant R306Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NL2
Type: protein
Length: 1,187 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Desferrioxamine E biosynthesis protein desd
UniProt: Q9L069
Ligands: CL
Pockets: 11 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Desferrioxamine E biosynthesis protein desd	protein	594	45% helix, 20% strand	Q9L069
B	Desferrioxamine E biosynthesis protein desd	protein	593	44% helix, 20% strand	Q9L069

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · chains A, B
GOL · Glycerol · additive · 11 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1198	0.85	0.86	113	GOL
2	1146	0.83	0.84	99	CL, GOL
3	770	0.77	0.81	57	GOL
4	465	0.76	0.84	49	GOL
5	56	0.49	0.86	19	empty

Interfaces

1 interface between chains.

A–B · 2006 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6NL2 · Apo NIS synthetase DesD variant R306Q · 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 Q9L069
Elsewhere: RCSB PDB 6NL2 · PDBe 6NL2 · UniProt Q9L069

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