Atomistry » Zinc » PDB 1bvt-1cao » 1cak
Atomistry »
  Zinc »
    PDB 1bvt-1cao »
      1cak »

Zinc in PDB 1cak: Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II

Enzymatic activity of Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II

All present enzymatic activity of Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II, PDB code: 1cak was solved by Y.Xue, A.Liljas, B.-H.Jonsson, S.Lindskog, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II (pdb code 1cak). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II, PDB code: 1cak:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1cak

Go back to Zinc Binding Sites List in 1cak
Zinc binding site 1 out of 2 in the Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:7.1
occ:1.00
O2 A:SO4500 2.1 17.4 1.0
ND1 A:HIS119 2.2 2.5 1.0
NE2 A:HIS96 2.2 2.0 1.0
NE2 A:HIS94 2.2 4.2 1.0
CE1 A:HIS119 2.9 2.0 1.0
O4 A:SO4500 2.9 16.5 1.0
CD2 A:HIS94 3.0 2.5 1.0
CD2 A:HIS96 3.0 2.0 1.0
S A:SO4500 3.0 17.0 1.0
CE1 A:HIS94 3.2 2.8 1.0
CE1 A:HIS96 3.2 3.0 1.0
CG A:HIS119 3.2 4.0 1.0
O3 A:SO4500 3.6 17.7 1.0
CB A:HIS119 3.6 2.0 1.0
OG1 A:THR199 3.9 8.2 1.0
NE2 A:HIS119 4.0 2.0 1.0
CG A:HIS94 4.2 2.9 1.0
CG A:HIS96 4.2 2.5 1.0
O1 A:SO4500 4.2 17.2 1.0
ND1 A:HIS94 4.2 4.8 1.0
CD2 A:HIS119 4.2 2.0 1.0
ND1 A:HIS96 4.3 2.6 1.0
O A:HOH292 4.5 17.5 1.0
CG2 A:THR200 4.9 13.0 1.0

Zinc binding site 2 out of 2 in 1cak

Go back to Zinc Binding Sites List in 1cak
Zinc binding site 2 out of 2 in the Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Analysis of the Zinc Hydroxide-Thr 199-Glu 106 Hydrogen Bonding Network in Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn362

b:21.1
occ:1.00
O A:HOH491 2.4 36.0 1.0
O A:HOH448 2.4 38.0 1.0
SG A:CYS206 2.9 8.4 0.2
O A:GLN137 2.9 7.9 1.0
CB A:CYS206 3.0 8.9 0.8
O A:VAL135 3.0 14.1 1.0
CB A:CYS206 3.1 7.2 0.2
C A:GLN137 3.4 9.9 1.0
N A:GLN137 3.4 11.3 1.0
O A:GLU205 3.4 7.8 1.0
C A:GLN136 3.4 13.1 1.0
CA A:CYS206 3.5 6.2 1.0
C A:GLU205 3.7 6.8 1.0
N A:CYS206 3.8 6.0 1.0
C A:VAL135 3.8 12.4 1.0
O A:GLN136 3.8 13.5 1.0
O A:HOH331 3.9 21.4 1.0
CA A:GLN136 3.9 13.2 1.0
CA A:GLN137 3.9 11.1 1.0
N A:PRO138 4.0 9.6 1.0
N A:GLN136 4.2 12.7 1.0
O A:HOH365 4.3 19.2 1.0
SG A:CYS206 4.3 10.2 0.8
CA A:PRO138 4.4 9.2 1.0
N A:GLU205 4.4 5.5 1.0
CA A:GLU205 4.6 5.9 1.0
CB A:LEU204 4.7 6.5 1.0
CA A:VAL135 4.9 11.0 1.0
C A:LEU204 4.9 4.7 1.0
C A:CYS206 5.0 5.7 1.0

Reference:

Y.Xue, A.Liljas, B.H.Jonsson, S.Lindskog. Structural Analysis of the Zinc Hydroxide-Thr-199-Glu-106 Hydrogen-Bond Network in Human Carbonic Anhydrase II. Proteins V. 17 93 1993.
ISSN: ISSN 0887-3585
PubMed: 7901850
DOI: 10.1002/PROT.340170112
Page generated: Sat Oct 12 22:59:58 2024

Last articles

F in 5TW3
F in 5TYK
F in 5TWN
F in 5TWM
F in 5TWO
F in 5TRG
F in 5TTO
F in 5TTH
F in 5TVJ
F in 5TRF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy