Chlorine in PDB 6wv7: Human Vkor with Chlorophacinone

All present enzymatic activity of Human Vkor with Chlorophacinone:
1.17.4.4;

The structure of Human Vkor with Chlorophacinone, PDB code: 6wv7 was solved by S.Liu, N.Sukumar, W.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.74 / 2.48
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	42.564, 82.567, 78.782, 93.39, 97.36, 104.21
R / Rfree (%)	20 / 24.5

The binding sites of Chlorine atom in the Human Vkor with Chlorophacinone (pdb code 6wv7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Vkor with Chlorophacinone, PDB code: 6wv7:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Vkor with Chlorophacinone


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Vkor with Chlorophacinone within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl400 b:42.9 occ:1.00 CL1 A:UAJ400 0.0 42.9 1.0 C11 A:UAJ400 1.8 40.5 1.0 C10 A:UAJ400 2.7 40.9 1.0 H101 A:UAJ400 2.8 48.8 1.0 C12 A:UAJ400 2.8 38.8 1.0 H121 A:UAJ400 2.9 46.4 1.0 OG A:SER259 3.2 29.4 1.0 O A:SER255 3.4 37.1 1.0 N A:SER259 3.7 32.3 1.0 ND2 A:ASN284 3.9 27.9 1.0 CE1 A:PHE205 3.9 39.9 1.0 C A:GLY258 3.9 35.0 1.0 C09 A:UAJ400 4.0 41.3 1.0 C13 A:UAJ400 4.1 37.2 1.0 CA A:SER259 4.1 31.5 1.0 CA A:SER255 4.2 31.4 1.0 CB A:SER259 4.2 28.3 1.0 C A:SER255 4.2 36.6 1.0 CA A:GLY258 4.3 30.6 1.0 O A:GLY258 4.4 42.1 1.0 CZ A:PHE205 4.4 35.1 1.0 CB A:SER255 4.5 32.3 1.0 C08 A:UAJ400 4.5 39.9 1.0 CD1 A:LEU262 4.6 24.5 1.0 H091 A:UAJ400 4.7 49.4 1.0 H131 A:UAJ400 4.8 44.4 1.0 N A:GLY258 5.0 30.8 1.0

Chlorine binding site 2 out of 2 in the Human Vkor with Chlorophacinone


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Vkor with Chlorophacinone within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl400 b:55.3 occ:1.00 CL1 B:UAJ400 0.0 55.3 1.0 C11 B:UAJ400 1.8 42.5 1.0 C10 B:UAJ400 2.7 41.1 1.0 H101 B:UAJ400 2.7 49.1 1.0 C12 B:UAJ400 2.8 40.0 1.0 H121 B:UAJ400 2.9 47.8 1.0 O B:SER255 3.4 36.5 1.0 OG B:SER259 3.5 41.4 1.0 O B:HOH595 3.6 50.1 1.0 N B:SER259 3.9 38.1 1.0 C B:GLY258 4.0 38.8 1.0 C09 B:UAJ400 4.0 42.2 1.0 CA B:SER255 4.0 39.4 1.0 ND2 B:ASN284 4.0 33.8 1.0 C13 B:UAJ400 4.1 37.3 1.0 C B:SER255 4.1 37.9 1.0 CA B:GLY258 4.1 38.8 1.0 CE1 B:PHE205 4.3 45.4 1.0 CB B:SER255 4.3 45.1 1.0 CA B:SER259 4.4 36.8 1.0 O B:GLY258 4.5 40.4 1.0 C08 B:UAJ400 4.5 39.9 1.0 CB B:SER259 4.5 40.2 1.0 CZ B:PHE205 4.6 47.8 1.0 H091 B:UAJ400 4.7 50.5 1.0 N B:GLY258 4.8 40.2 1.0 O B:HOH599 4.8 44.0 1.0 CD1 B:LEU262 4.8 36.0 1.0 H131 B:UAJ400 4.8 44.6 1.0

S.Liu, S.Li, G.Shen, N.Sukumar, A.M.Krezel, W.Li. Structural Basis of Antagonizing the Vitamin K Catalytic Cycle For Anticoagulation. Science 2020.
ISSN: ESSN 1095-9203
PubMed: 33154105
DOI: 10.1126/SCIENCE.ABC5667