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Zinc in PDB 2x7t: Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors.

Enzymatic activity of Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors.

All present enzymatic activity of Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors.:
4.2.1.1;

Protein crystallography data

The structure of Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors., PDB code: 2x7t was solved by G.E.Cozier, M.P.Leese, M.D.Lloyd, M.D.Baker, N.Thiyagarajan, K.R.Acharya, B.V.L.Potter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.99 / 1.89
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.256, 40.832, 72.697, 90.00, 104.49, 90.00
R / Rfree (%) 21.1 / 24.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors. (pdb code 2x7t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors., PDB code: 2x7t:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2x7t

Go back to Zinc Binding Sites List in 2x7t
Zinc binding site 1 out of 2 in the Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1263

b:11.0
occ:1.00
 NAD A:WZB1261 2.1 14.1 1.0
NE2 A:HIS94 2.2 10.6 1.0
ND1 A:HIS119 2.2 10.4 1.0
NE2 A:HIS96 2.2 10.7 1.0
CD2 A:HIS94 2.9 11.3 1.0
CD2 A:HIS96 2.9 8.8 1.0
SBD A:WZB1261 3.0 13.7 1.0
CE1 A:HIS119 3.1 9.7 1.0
OAH A:WZB1261 3.1 15.3 1.0
CG A:HIS119 3.2 10.1 1.0
CE1 A:HIS94 3.3 10.2 1.0
CE1 A:HIS96 3.4 9.7 1.0
OAS A:WZB1261 3.6 15.6 1.0
CB A:HIS119 3.6 8.1 1.0
OE1 A:GLU106 3.8 9.2 1.0
OG1 A:THR198 3.8 9.6 1.0
CG A:HIS94 4.2 10.5 1.0
CAM A:WZB1261 4.2 16.5 1.0
CG A:HIS96 4.2 8.2 1.0
NE2 A:HIS119 4.2 8.6 1.0
OAG A:WZB1261 4.3 15.4 1.0
ND1 A:HIS94 4.3 9.8 1.0
CAX A:WZB1261 4.3 16.9 1.0
CD2 A:HIS119 4.3 8.3 1.0
ND1 A:HIS96 4.4 7.5 1.0
CD A:GLU106 4.8 10.0 1.0

Zinc binding site 2 out of 2 in 2x7t

Go back to Zinc Binding Sites List in 2x7t
Zinc binding site 2 out of 2 in the Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structures of Human Carbonic Anhydrase II Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1264

b:80.1
occ:1.00
 NE2 A:HIS64 2.1 24.5 1.0
NE2 A:HIS4 2.2 26.1 1.0
CE1 A:HIS64 3.0 22.1 1.0
CD2 A:HIS4 3.1 26.0 1.0
CD2 A:HIS64 3.2 21.7 1.0
CE1 A:HIS4 3.2 25.2 1.0
NE1 A:TRP5 4.1 16.4 1.0
ND1 A:HIS64 4.1 22.8 1.0
CG A:HIS64 4.2 23.0 1.0
CE2 A:TRP5 4.3 15.4 1.0
ND1 A:HIS4 4.3 25.0 1.0
CG A:HIS4 4.3 24.9 1.0
CZ2 A:TRP5 4.3 15.8 1.0
O A:ASN62 4.4 22.3 1.0
NZ A:LYS169 4.5 29.3 1.0
O A:HOH2001 4.8 32.0 1.0
CD1 A:TRP5 4.8 17.7 1.0
O A:TRP5 5.0 15.3 1.0

Reference:

G.E.Cozier, M.P.Leese, M.D.Lloyd, M.D.Baker, N.Thiyagarajan, K.R.Acharya, B.V.L.Potter. Structures of Human Carbonic Anhydrase II/Inhibitor Complexes Reveal A Second Binding Site For Steroidal and Non-Steroidal Inhibitors. Biochemistry V. 49 3464 2010.
ISSN: ISSN 0006-2960
PubMed: 20297840
DOI: 10.1021/BI902178W
Page generated: Thu Oct 17 05:11:12 2024

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