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Copper in PDB 2fos: Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors

Enzymatic activity of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors

All present enzymatic activity of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors, PDB code: 2fos was solved by K.M.Jude, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 80.00 / 1.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.444, 41.640, 72.278, 90.00, 104.24, 90.00
R / Rfree (%) 12.7 / 15.3

Copper Binding Sites:

The binding sites of Copper atom in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors (pdb code 2fos). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors, PDB code: 2fos:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2fos

Go back to Copper Binding Sites List in 2fos
Copper binding site 1 out of 2 in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu303

b:44.0
occ:0.74
NE2 A:HIS64 2.4 27.9 0.7
CD2 A:HIS64 3.2 21.1 0.7
CE1 A:HIS64 3.5 25.8 0.7
CD2 A:HIS64 3.9 14.4 0.3
O A:HOH687 3.9 37.2 1.0
NE2 A:HIS64 4.0 15.9 0.3
O A:ASN62 4.3 12.9 1.0
CG A:HIS64 4.4 17.5 0.7
ND1 A:HIS64 4.5 22.1 0.7
NE1 A:TRP5 4.6 16.9 1.0
CZ2 A:TRP5 4.7 15.2 1.0
CE2 A:TRP5 4.8 13.7 1.0
O A:HOH662 5.0 33.8 0.5

Copper binding site 2 out of 2 in 2fos

Go back to Copper Binding Sites List in 2fos
Copper binding site 2 out of 2 in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu304

b:34.0
occ:0.75
ND1 A:HIS3 1.9 33.0 1.0
CA A:SER2 2.0 36.8 0.3
N A:HIS3 2.2 40.7 1.0
C A:SER2 2.4 37.0 0.3
CE1 A:HIS3 2.7 40.7 1.0
OG A:SER2 2.7 38.0 0.3
CB A:SER2 2.8 34.1 0.3
N A:SER2 3.1 47.4 0.3
CG A:HIS3 3.1 36.5 1.0
CA A:HIS3 3.4 34.4 1.0
O A:HIS3 3.6 26.9 1.0
O A:SER2 3.7 29.8 0.3
CB A:HIS3 3.7 38.4 1.0
O A:HOH547 3.7 35.9 1.0
NE2 A:HIS3 3.9 41.8 1.0
C A:HIS3 4.0 26.0 1.0
CD2 A:HIS3 4.1 37.3 1.0

Reference:

K.M.Jude, A.L.Banerjee, M.K.Haldar, S.Manokaran, B.Roy, S.Mallik, D.K.Srivastava, D.W.Christianson. Ultrahigh Resolution Crystal Structures of Human Carbonic Anhydrases I and II Complexed with Two-Prong Inhibitors Reveal the Molecular Basis of High Affinity. J.Am.Chem.Soc. V. 128 3011 2006.
ISSN: ISSN 0002-7863
PubMed: 16506782
DOI: 10.1021/JA057257N
Page generated: Thu Sep 3 16:38:03 2020
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