Zinc in PDB 6cen: Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21

All present enzymatic activity of Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21:
2.1.1.43;

The structure of Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21, PDB code: 6cen was solved by P.A.Boriack-Sjodin, K.Swinger, N.A.Farrow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.29 / 1.61
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.870, 62.660, 48.600, 90.00, 107.92, 90.00
R / Rfree (%)	17.9 / 21.5

The binding sites of Zinc atom in the Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21 (pdb code 6cen). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21, PDB code: 6cen:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1302 b:23.5 occ:1.00 SG A:CYS1108 2.3 24.6 1.0 SG A:CYS1098 2.3 24.7 1.0 SG A:CYS1114 2.3 20.5 1.0 SG A:CYS1100 2.4 29.5 1.0 CB A:CYS1098 3.2 25.5 1.0 CB A:CYS1100 3.2 31.9 1.0 CB A:CYS1114 3.3 23.2 1.0 CB A:CYS1108 3.3 24.3 1.0 CA A:CYS1108 3.7 25.0 1.0 ZN A:ZN1303 3.8 22.5 1.0 CA A:CYS1114 3.9 25.2 1.0 N A:CYS1108 4.1 25.2 1.0 O A:HOH1537 4.2 26.3 1.0 N A:CYS1100 4.2 33.6 1.0 CA A:CYS1100 4.3 33.8 1.0 SG A:CYS1123 4.4 18.7 1.0 CA A:CYS1098 4.6 27.4 1.0 SG A:CYS1128 4.7 25.8 1.0 C A:CYS1114 4.7 25.2 1.0 O A:HOH1530 4.8 21.6 1.0 N A:LEU1115 4.8 26.2 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1303 b:22.5 occ:1.00 SG A:CYS1128 2.3 25.8 1.0 SG A:CYS1134 2.3 25.7 1.0 SG A:CYS1123 2.3 18.7 1.0 SG A:CYS1108 2.3 24.6 1.0 CB A:CYS1123 3.1 18.9 1.0 CB A:CYS1108 3.3 24.3 1.0 CB A:CYS1134 3.3 26.1 1.0 CB A:CYS1128 3.4 26.9 1.0 ZN A:ZN1302 3.8 23.5 1.0 O A:HOH1530 3.9 21.6 1.0 SG A:CYS1098 4.0 24.7 1.0 CA A:CYS1134 4.3 27.0 1.0 CB A:ASN1136 4.4 18.9 1.0 CA A:CYS1123 4.6 18.7 1.0 CA A:CYS1128 4.7 29.0 1.0 CA A:CYS1108 4.7 25.0 1.0 CB A:ALA1130 4.7 33.2 1.0 SG A:CYS1114 4.9 20.5 1.0 N A:ASN1136 4.9 22.0 1.0 C A:CYS1134 5.0 25.1 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of WHSC1L1 in Complex with Inhibitor PEP21 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1304 b:11.9 occ:1.00 SG A:CYS1280 2.3 11.1 1.0 SG A:CYS1226 2.3 11.3 1.0 SG A:CYS1273 2.3 12.1 1.0 SG A:CYS1275 2.3 11.4 1.0 CB A:CYS1280 3.3 12.1 1.0 CB A:CYS1273 3.4 14.6 1.0 CB A:CYS1275 3.4 11.2 1.0 CB A:CYS1226 3.4 11.4 1.0 CA A:CYS1280 3.7 11.9 1.0 N A:CYS1226 3.9 10.5 1.0 N A:CYS1275 4.0 11.2 1.0 CA A:CYS1275 4.2 11.7 1.0 O A:HOH1506 4.3 14.1 1.0 CA A:CYS1226 4.3 11.0 1.0 NE2 A:HIS1224 4.3 11.4 1.0 N A:SER1281 4.4 13.5 1.0 CD2 A:HIS1224 4.4 11.4 1.0 C A:CYS1280 4.5 13.2 1.0 CA A:CYS1273 4.6 14.7 1.0 C A:CYS1273 4.7 14.8 1.0 O A:CYS1273 4.8 15.7 1.0 N A:GLY1276 4.9 12.1 1.0 N A:CYS1280 4.9 11.8 1.0 N A:GLY1282 4.9 16.9 1.0 C A:SER1225 4.9 11.0 1.0 C A:CYS1275 4.9 11.9 1.0 O A:HOH1422 5.0 24.3 1.0

M.J.Morrison, P.A.Boriack-Sjodin, K.K.Swinger, T.J.Wigle, D.Sadalge, K.W.Kuntz, M.P.Scott, W.P.Janzen, R.Chesworth, K.W.Duncan, D.M.Harvey, J.W.Lampe, L.H.Mitchell, R.A.Copeland. Identification of A Peptide Inhibitor For the Histone Methyltransferase WHSC1. Plos One V. 13 97082 2018.
ISSN: ESSN 1932-6203
PubMed: 29742153
DOI: 10.1371/JOURNAL.PONE.0197082