MolNFT v1 · #178469 · protein

Friedel-crafts alkylation enzyme cylk mutant H391A

7FH8: “Friedel-crafts alkylation enzyme cylk mutant H391A”. X-ray diffraction, 4 ligands (4PJ, CA, MG), 4 pockets (best druggability 0.85). MolNFT v1 #178469 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7FH8
Type: protein
Length: 653 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cylk
UniProt: A0A1Y0K711
Ligands: 4PJ, CA, MG, CL
Pockets: 4 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cylk	protein	653	8% helix, 40% strand	A0A1Y0K711

Ligands and binding sites

4PJ · 2-[(5S,10S)-11-[3,5-bis(oxidanyl)phenyl]-10-methyl-undecan-5-yl]-5-[(2S,7R)-7-fluoranyl-2-methyl-undecyl]benzene-1,3-diol · ligand · chains A
CA · Calcium ion · metal · 12 copies · chains A
MG · Magnesium ion · metal · 5 copies · chains A
CL · Chloride ion · ion · 7 copies · chains A

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

Pockets

4 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	812	0.85	0.88	80	4PJ, CL
2	416	0.69	0.81	43	MG, CA
3	82	0.35	0.76	18	empty
4	55	0.30	0.75	17	empty

Compared structures

7FH8 · Friedel-Crafts alkylation enzyme CylK mutant H391A · 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 A0A1Y0K711
Elsewhere: RCSB PDB 7FH8 · PDBe 7FH8 · UniProt A0A1Y0K711

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