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Crystal structure of the anst-D7L1-leukotriene C4 complex

Analyse Crystal structure of the anst-D7L1-leukotriene C4 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NHI
Type: protein
Length: 295 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D7 protein
UniProt: Q95NY5
Ligands: EAH, SO4
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D7 protein	protein	295	59% helix, 3% strand	Q95NY5

Ligands and binding sites

EAH · (5S,7E,9E,11Z,14Z)-5-hydroxyicosa-7,9,11,14-tetraenoic acid · ligand · chains A
SO4 · Sulfate 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

3 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	272	0.69	0.84	44	EAH
2	335	0.53	0.74	34	empty
3	50	0.36	0.80	13	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3NHI · Crystal structure of the AnSt-D7L1-leukotriene C4 complex · 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 Q95NY5
Elsewhere: RCSB PDB 3NHI · PDBe 3NHI · UniProt Q95NY5

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