MolNFT v1 · #167299 · protein

Crystal structures of flap bound to mk-866

6VGI: “Crystal structures of flap bound to mk-866”. X-ray diffraction, 2 ligands (QY7, SO4). MolNFT v1 #167299 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6VGI
Type: protein
Length: 870 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P20292
Ligands: QY7, SO4

Structure

x-ray diffraction · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	139	—	P20292
B	—	protein	140	—	P20292
C	—	protein	143	—	P20292
D	—	protein	150	—	P20292
E	—	protein	144	—	P20292
F	—	protein	154	—	P20292

Ligands and binding sites

QY7 · 3-[3-(tert-butylsulfanyl)-1-[(4-chlorophenyl)methyl]-5-(propan-2-yl)-1H-indol-2-yl]-2,2-dimethylpropanoic acid · ligand · 6 copies · chains A, F, B, C, D, E
SO4 · Sulfate ion · ion · 5 copies · chains A, B, C, E, F

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

Compared structures

6VGI · Crystal Structures of FLAP bound to MK-866 · the same entry in another collection · chain F against F, TM-score 1.00
P20292 · AlphaFold monomer V2.0 prediction for arachidonate 5-lipoxygenase- activating protein… · a predicted model of the same protein · chain A against A, TM-score 0.86

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 P20292
Elsewhere: RCSB PDB 6VGI · PDBe 6VGI · UniProt P20292

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