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Copper in PDB 2fou: 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: 2fou 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) 60.00 / 0.99
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.557, 41.704, 72.710, 90.00, 104.38, 90.00
R / Rfree (%) 12.3 / 13.5

Other elements in 2fou:

The structure of Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors also contains other interesting chemical elements:

Mercury (Hg) 1 atom
Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Human Carbonic Anhydrase II Complexed with Two-Prong Inhibitors (pdb code 2fou). 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: 2fou:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2fou

Go back to Copper Binding Sites List in 2fou
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:Cu302

b:19.4
occ:0.52
ND1 A:HIS3 1.9 25.3 1.0
N A:HIS3 2.0 29.2 1.0
OG A:SER2 2.2 52.8 1.0
CG A:HIS3 2.8 25.7 1.0
C A:SER2 2.9 32.7 1.0
CE1 A:HIS3 3.0 24.5 1.0
CA A:SER2 3.0 48.3 1.0
CA A:HIS3 3.0 23.6 1.0
CB A:SER2 3.0 52.1 1.0
CB A:HIS3 3.1 25.9 1.0
O A:HIS3 3.6 20.4 1.0
C A:HIS3 3.7 20.2 1.0
O A:HOH602 3.7 19.3 0.5
CD2 A:HIS3 4.0 27.3 1.0
NE2 A:HIS3 4.0 27.4 1.0
O A:SER2 4.0 34.5 1.0
N A:SER2 4.4 47.4 1.0
O A:HOH641 4.9 45.4 0.5
N A:HIS4 5.0 20.4 1.0

Copper binding site 2 out of 2 in 2fou

Go back to Copper Binding Sites List in 2fou
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:Cu303

b:55.3
occ:0.82
CU A:B22303 0.0 55.3 0.8
C23 A:B22303 1.7 68.0 0.8
NE2 A:HIS4 1.8 35.6 1.0
OXD A:B22303 2.0 69.3 0.8
OXB A:B22303 2.0 57.2 0.8
C24 A:B22303 2.1 68.6 0.8
N20 A:B22303 2.1 64.2 0.8
N17 A:B22303 2.4 56.3 0.8
CE1 A:HIS4 2.8 36.1 1.0
C22 A:B22303 2.8 63.3 0.8
C21 A:B22303 2.8 64.6 0.8
C19 A:B22303 2.9 61.4 0.8
CD2 A:HIS4 2.9 30.1 1.0
C18 A:B22303 2.9 57.7 0.8
C15 A:B22303 3.1 48.1 0.8
OXC A:B22303 3.3 77.9 0.8
C14 A:B22303 3.7 46.7 0.8
C16 A:B22303 3.8 40.6 0.8
ND1 A:HIS4 3.9 28.3 1.0
O18 A:B22303 4.0 66.2 0.8
CG A:HIS4 4.0 23.1 1.0
OXA A:B22303 4.0 63.1 0.8
C13 A:B22303 4.8 42.1 0.8
C11 A:B22303 4.9 37.3 0.8

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: Sun Dec 13 11:04:37 2020

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