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Copper in PDB 2fov: 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: 2fov 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) 50.00 / 1.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.362, 41.482, 72.234, 90.00, 104.34, 90.00
R / Rfree (%) 14.3 / 18.7

Copper Binding Sites:

The binding sites of Copper atom in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors (pdb code 2fov). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors, PDB code: 2fov:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 2fov

Go back to Copper Binding Sites List in 2fov
Copper binding site 1 out of 3 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:Cu304

b:52.6
occ:1.00
ND1 A:HIS3 1.9 53.8 1.0
N A:HIS3 2.2 46.2 1.0
CB A:SER2 2.5 52.2 0.5
CB A:SER2 2.6 52.4 0.5
CA A:SER2 2.7 53.8 1.0
C A:SER2 2.8 48.6 1.0
CE1 A:HIS3 2.8 56.1 1.0
OG A:SER2 2.8 55.8 0.5
CG A:HIS3 3.0 50.9 1.0
CA A:HIS3 3.4 41.8 1.0
OG A:SER2 3.5 51.1 0.5
CB A:HIS3 3.5 46.1 1.0
O A:HIS3 3.7 30.7 1.0
O A:HOH568 3.8 40.9 1.0
NE2 A:HIS3 4.0 55.9 1.0
O A:SER2 4.0 53.0 1.0
C A:HIS3 4.0 37.5 1.0
CD2 A:HIS3 4.1 52.4 1.0
N A:SER2 4.1 60.6 1.0

Copper binding site 2 out of 3 in 2fov

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Copper binding site 2 out of 3 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:Cu301

b:29.7
occ:1.00
CU A:B30301 0.0 29.7 1.0
OXC A:B30301 1.9 52.5 1.0
OXB A:B30301 2.0 35.9 1.0
NE2 A:HIS64 2.0 18.4 0.7
N11 A:B30301 2.0 39.6 1.0
C14 A:B30301 2.2 48.8 1.0
C15 A:B30301 2.3 56.0 1.0
O A:HOH609 2.5 24.7 1.0
C10 A:B30301 2.6 39.0 1.0
C12 A:B30301 2.7 42.7 1.0
C13 A:B30301 2.7 33.1 1.0
CE1 A:HIS64 2.9 17.5 0.7
CD2 A:HIS64 3.1 16.9 0.7
OXD A:B30301 3.5 69.0 1.0
C9 A:B30301 3.8 31.5 1.0
OXA A:B30301 3.9 28.6 1.0
N8 A:B30301 3.9 22.1 1.0
ND1 A:HIS64 4.0 17.0 0.7
ND2 A:ASN62 4.1 17.0 1.0
CD2 A:HIS64 4.2 16.7 0.3
CG A:HIS64 4.2 14.6 0.7
O A:HOH482 4.4 27.3 1.0
OG1 A:THR200 4.5 14.6 1.0
CZ2 A:TRP5 4.6 16.8 1.0
CG A:ASN62 4.6 12.6 1.0
C7 A:B30301 4.8 14.6 1.0
O A:HOH451 4.8 18.1 1.0
O A:HOH535 4.9 27.5 1.0
O A:PRO201 4.9 15.7 1.0
CG A:HIS64 4.9 13.6 0.3

Copper binding site 3 out of 3 in 2fov

Go back to Copper Binding Sites List in 2fov
Copper binding site 3 out of 3 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 3 of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu303

b:43.1
occ:0.81
CU A:B30303 0.0 43.1 0.8
C12 A:B30303 1.9 53.1 0.8
OXB A:B30303 2.0 67.7 0.8
OXC A:B30303 2.0 56.1 0.8
C13 A:B30303 2.0 61.5 0.8
N11 A:B30303 2.1 43.5 0.8
C10 A:B30303 2.7 37.0 0.8
C15 A:B30303 2.9 55.5 0.8
C14 A:B30303 2.9 49.5 0.8
OXA A:B30303 3.0 71.0 0.8
NE2 A:HIS4 3.0 49.1 0.5
CD2 A:HIS4 3.3 44.1 0.5
O A:HOH664 3.4 49.3 0.5
OXD A:B30303 4.1 58.8 0.8
CE1 A:HIS4 4.2 46.8 0.5
C9 A:B30303 4.2 27.5 0.8
CG A:HIS4 4.5 39.5 0.5
O A:HOH421 4.5 23.0 1.0
CE1 A:HIS4 4.6 28.1 0.5
ND1 A:HIS4 4.7 27.2 0.5
ND1 A:HIS4 4.9 41.9 0.5

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 16:38:17 2020
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