Fluorine in PDB 4wua: Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340

All present enzymatic activity of Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340:
2.7.11.1;

The structure of Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340, PDB code: 4wua was solved by M.Hoshina, T.Ikura, T.Hosoya, M.Hagiwara, N.Ito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.87 / 2.00
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	75.132, 75.132, 310.623, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 23.6

The binding sites of Fluorine atom in the Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340 (pdb code 4wua). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340, PDB code: 4wua:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340 within 5.0Å range: probe atom residue distance (Å) B Occ A:F701 b:48.7 occ:1.00 F2 A:3UL701 0.0 48.7 1.0 C9 A:3UL701 1.3 40.3 1.0 F1 A:3UL701 2.1 41.6 1.0 F A:3UL701 2.1 39.5 1.0 C8 A:3UL701 2.3 32.6 1.0 C10 A:3UL701 2.8 34.5 1.0 CE2 A:TYR227 3.3 42.1 1.0 C7 A:3UL701 3.5 29.9 1.0 CD2 A:TYR227 3.8 41.8 1.0 CD1 A:LEU231 3.9 45.9 1.0 NE2 A:HIS170 4.0 45.4 1.0 CG2 A:VAL223 4.0 34.7 1.0 C11 A:3UL701 4.1 32.2 1.0 CE1 A:HIS170 4.4 38.4 1.0 CG1 A:VAL223 4.4 38.1 1.0 CZ A:TYR227 4.4 45.0 1.0 CA A:GLY169 4.5 28.3 1.0 CD2 A:LEU86 4.5 36.9 1.0 CD2 A:HIS170 4.6 41.6 1.0 OH A:TYR227 4.7 52.1 1.0 C6 A:3UL701 4.7 29.6 1.0 CB A:VAL223 4.9 39.5 1.0 C12 A:3UL701 5.0 31.6 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340 within 5.0Å range: probe atom residue distance (Å) B Occ A:F701 b:39.5 occ:1.00 F A:3UL701 0.0 39.5 1.0 C9 A:3UL701 1.3 40.3 1.0 F2 A:3UL701 2.1 48.7 1.0 F1 A:3UL701 2.1 41.6 1.0 C8 A:3UL701 2.4 32.6 1.0 C7 A:3UL701 2.8 29.9 1.0 CG1 A:VAL167 3.5 40.9 1.0 CG2 A:VAL223 3.5 34.7 1.0 CA A:GLY169 3.5 28.3 1.0 O A:LEU168 3.6 31.2 1.0 C10 A:3UL701 3.6 34.5 1.0 N A:GLY169 3.8 25.8 1.0 C A:LEU168 3.8 31.2 1.0 C6 A:3UL701 4.2 29.6 1.0 CG1 A:ILE228 4.3 39.5 1.0 N A:LEU168 4.4 34.8 1.0 O A:3UL701 4.5 28.9 1.0 C A:GLY169 4.5 27.8 1.0 CG1 A:VAL223 4.6 38.1 1.0 CD1 A:ILE228 4.7 40.0 1.0 CB A:VAL223 4.7 39.5 1.0 C11 A:3UL701 4.7 32.2 1.0 CA A:LEU168 4.8 34.8 1.0 CB A:VAL167 4.9 38.2 1.0 CD2 A:TYR227 4.9 41.8 1.0 C12 A:3UL701 5.0 31.6 1.0 CE2 A:TYR227 5.0 42.1 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Human SRPK1 Complexed to An Inhibitor SRPIN340 within 5.0Å range: probe atom residue distance (Å) B Occ A:F701 b:41.6 occ:1.00 F1 A:3UL701 0.0 41.6 1.0 C9 A:3UL701 1.3 40.3 1.0 F2 A:3UL701 2.1 48.7 1.0 F A:3UL701 2.1 39.5 1.0 C8 A:3UL701 2.3 32.6 1.0 C7 A:3UL701 3.1 29.9 1.0 CD2 A:LEU86 3.2 36.9 1.0 C10 A:3UL701 3.2 34.5 1.0 CD1 A:LEU86 3.7 37.4 1.0 CD1 A:LEU231 3.7 45.9 1.0 CG1 A:VAL167 3.9 40.9 1.0 CG A:LEU86 4.0 35.9 1.0 C6 A:3UL701 4.3 29.6 1.0 C11 A:3UL701 4.4 32.2 1.0 CG1 A:ILE228 4.6 39.5 1.0 CE2 A:TYR227 4.9 42.1 1.0 CB A:LEU86 4.9 32.3 1.0 C12 A:3UL701 4.9 31.6 1.0 CD1 A:LEU96 5.0 32.1 1.0

S.Morooka, M.Hoshina, I.Kii, T.Okabe, H.Kojima, N.Inoue, Y.Okuno, M.Denawa, S.Yoshida, J.Fukuhara, K.Ninomiya, T.Ikura, T.Furuya, T.Nagano, K.Noda, S.Ishida, T.Hosoya, N.Ito, N.Yoshimura, M.Hagiwara. Identification of A Dual Inhibitor of SRPK1 and CK2 That Attenuates Pathological Angiogenesis of Macular Degeneration in Mice Mol.Pharmacol. V. 88 316 2015.
ISSN: ESSN 1521-0111
PubMed: 25993998
DOI: 10.1124/MOL.114.097345