Zinc in PDB 4y0j: H/D Exchanged Human Carbonic Anhydrase II pH 6 Room Temperature Neutron Crystal Structure.

All present enzymatic activity of H/D Exchanged Human Carbonic Anhydrase II pH 6 Room Temperature Neutron Crystal Structure.:
4.2.1.1;

The binding sites of Zinc atom in the H/D Exchanged Human Carbonic Anhydrase II pH 6 Room Temperature Neutron Crystal Structure. (pdb code 4y0j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the H/D Exchanged Human Carbonic Anhydrase II pH 6 Room Temperature Neutron Crystal Structure., PDB code: 4y0j:

Zinc binding site 1 out of 1 in the H/D Exchanged Human Carbonic Anhydrase II pH 6 Room Temperature Neutron Crystal Structure.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of H/D Exchanged Human Carbonic Anhydrase II pH 6 Room Temperature Neutron Crystal Structure. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:28.4 occ:1.00 O A:DOD459 2.0 38.6 1.0 NE2 A:HIS96 2.2 25.0 1.0 ND1 A:HIS119 2.2 28.6 1.0 D2 A:DOD459 2.4 41.3 1.0 NE2 A:HIS94 2.4 27.2 1.0 D1 A:DOD459 2.8 41.6 1.0 D2 A:DOD461 3.0 74.6 1.0 CE1 A:HIS119 3.0 27.0 1.0 CD2 A:HIS96 3.0 26.2 1.0 HE1 A:HIS119 3.1 29.7 1.0 HD2 A:HIS96 3.1 25.1 1.0 CD2 A:HIS94 3.1 27.9 1.0 HD2 A:HIS94 3.2 26.3 1.0 HB2 A:HIS119 3.3 27.9 1.0 CE1 A:HIS96 3.3 25.7 1.0 CG A:HIS119 3.3 29.1 1.0 CE1 A:HIS94 3.5 28.6 1.0 HE1 A:HIS96 3.6 24.8 1.0 DG1 A:THR199 3.7 29.0 0.8 OG1 A:THR199 3.7 30.1 1.0 D1 A:DOD461 3.7 74.1 1.0 O A:DOD461 3.8 73.6 1.0 CB A:HIS119 3.8 26.0 1.0 HE1 A:HIS94 3.8 29.1 1.0 OE1 A:GLU106 4.0 21.4 1.0 HB3 A:HIS119 4.0 28.2 1.0 NE2 A:HIS119 4.1 29.6 1.0 HH2 A:TRP209 4.2 29.1 1.0 O A:DOD495 4.2 65.3 1.0 CG A:HIS96 4.2 27.6 1.0 CD2 A:HIS119 4.3 29.3 1.0 CG A:HIS94 4.3 26.5 1.0 ND1 A:HIS96 4.3 24.1 1.0 O A:DOD460 4.4 75.0 1.0 ND1 A:HIS94 4.5 29.9 1.0 D2 A:DOD503 4.6 65.9 1.0 D2 A:DOD495 4.7 65.9 1.0 HG22 A:THR200 4.7 27.6 1.0 CD A:GLU106 4.8 24.4 1.0 D A:THR199 4.8 29.1 0.9 D1 A:DOD495 4.9 65.8 1.0 DE2 A:HIS119 5.0 28.9 0.5 HG22 A:THR199 5.0 26.6 1.0 D2 A:DOD460 5.0 75.0 1.0

R.Michalczyk, C.J.Unkefer, J.P.Bacik, T.E.Schrader, A.Ostermann, A.Y.Kovalevsky, R.Mckenna, S.Z.Fisher. Joint Neutron Crystallographic and uc(Nmr) Solution Studies of Tyr Residue Ionization and Hydrogen Bonding: Implications For Enzyme-Mediated Proton Transfer. Proc.Natl.Acad.Sci.Usa V. 112 5673 2015.
ISSN: ESSN 1091-6490
PubMed: 25902526
DOI: 10.1073/PNAS.1502255112