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Copper in PDB 2foy: Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor

Enzymatic activity of Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor

All present enzymatic activity of Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor, PDB code: 2foy was solved by K.M.Jude, A.L.Banerjee, M.K.Haldar, S.Manokaran, B.Roy, S.Mallik, D.K.Srivastava, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.00 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.219, 72.608, 121.949, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 24.3

Other elements in 2foy:

The structure of Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor (pdb code 2foy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor, PDB code: 2foy:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 2foy

Go back to Copper Binding Sites List in 2foy
Copper binding site 1 out of 6 in the Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor


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 I Complexed with A Two-Prong Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu311

b:51.9
occ:1.00
 CU A:B30311 0.0 51.9 1.0
OXB A:B30311 2.0 54.0 1.0
OXC A:B30311 2.0 53.8 1.0
N11 A:B30311 2.3 52.5 1.0
C14 A:B30311 2.4 53.3 1.0
NE2 A:HIS200 2.4 24.9 1.0
O A:HOH958 2.5 30.0 1.0
C15 A:B30311 2.6 53.6 1.0
C13 A:B30311 2.7 54.5 1.0
C12 A:B30311 2.8 53.4 1.0
N8 A:B30311 3.0 40.1 1.0
C10 A:B30311 3.1 49.6 1.0
C9 A:B30311 3.2 45.3 1.0
CE1 A:HIS200 3.3 25.5 1.0
CD2 A:HIS200 3.5 24.4 1.0
OXD A:B30311 3.8 54.8 1.0
OXA A:B30311 3.9 55.6 1.0
C7 A:B30311 4.1 37.4 1.0
O A:PRO201 4.4 23.4 1.0
ND1 A:HIS200 4.4 23.1 1.0
NE2 A:HIS64 4.5 19.8 1.0
CG A:HIS200 4.6 22.5 1.0
C1 A:B30311 4.6 34.0 1.0
C2 A:B30311 4.7 32.0 1.0
CE1 A:HIS67 4.8 22.3 1.0
CZ2 A:TRP5 4.8 23.9 1.0
CE1 A:HIS64 5.0 19.5 1.0
O A:HOH718 5.0 36.5 1.0
O7 A:B30311 5.0 37.5 1.0

Copper binding site 2 out of 6 in 2foy

Go back to Copper Binding Sites List in 2foy
Copper binding site 2 out of 6 in the Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor


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 I Complexed with A Two-Prong Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu313

b:33.6
occ:1.00
 CU A:B30313 0.0 33.6 1.0
OXB A:B30313 2.0 37.9 0.6
OXC A:B30313 2.0 37.2 0.6
N11 A:B30313 2.3 36.3 0.6
C14 A:B30313 2.4 36.1 0.6
NE2 A:HIS243 2.5 25.6 1.0
C15 A:B30313 2.6 36.1 0.6
C13 A:B30313 2.7 37.8 0.6
C12 A:B30313 2.8 37.1 0.6
N8 A:B30313 3.0 37.7 0.6
C10 A:B30313 3.2 36.6 0.6
O A:HOH839 3.2 46.8 1.0
CD2 A:HIS243 3.2 24.6 1.0
C9 A:B30313 3.4 36.5 0.6
CE1 A:HIS243 3.6 24.2 1.0
C7 A:B30313 3.7 38.0 0.6
C2 A:B30313 3.8 37.2 0.6
OXD A:B30313 3.8 37.6 0.6
OXA A:B30313 3.9 40.4 0.6
C1 A:B30313 4.1 38.0 0.6
CG A:HIS243 4.5 23.1 1.0
O7 A:B30313 4.5 40.0 0.6
ND1 A:HIS243 4.6 23.9 1.0
CB A:GLN242 4.8 30.1 1.0
C3 A:B30313 4.9 36.2 0.6

Copper binding site 3 out of 6 in 2foy

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Copper binding site 3 out of 6 in the Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor


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 I Complexed with A Two-Prong Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu315

b:37.5
occ:1.00
 CU A:B30315 0.0 37.5 1.0
OXB A:B30315 2.0 38.4 0.6
OXC A:B30315 2.0 38.9 0.6
N11 A:B30315 2.3 37.9 0.6
C14 A:B30315 2.4 37.8 0.6
NE2 A:HIS103 2.4 47.1 1.0
C15 A:B30315 2.6 37.9 0.6
C13 A:B30315 2.7 38.4 0.6
C12 A:B30315 2.8 38.3 0.6
N8 A:B30315 3.0 38.5 0.6
C10 A:B30315 3.2 37.9 0.6
CD2 A:HIS103 3.2 45.3 1.0
C9 A:B30315 3.4 37.6 0.6
CE1 A:HIS103 3.5 47.5 1.0
C7 A:B30315 3.6 39.3 0.6
OXD A:B30315 3.8 39.1 0.6
OXA A:B30315 3.9 39.0 0.6
C1 A:B30315 4.1 39.3 0.7
NZ A:LYS113 4.1 41.3 1.0
C2 A:B30315 4.1 39.1 0.7
OE1 A:GLU102 4.3 60.6 1.0
O7 A:B30315 4.4 40.4 0.6
CD A:GLU102 4.4 56.1 1.0
CG A:HIS103 4.4 42.3 1.0
ND1 A:HIS103 4.5 45.2 1.0
CG A:GLU102 4.7 49.5 1.0
OE2 A:GLU102 4.8 60.3 1.0

Copper binding site 4 out of 6 in 2foy

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Copper binding site 4 out of 6 in the Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu312

b:57.9
occ:1.00
 CU B:B30312 0.0 57.9 1.0
OXB B:B30312 2.0 59.3 0.9
OXC B:B30312 2.0 59.2 0.9
N11 B:B30312 2.3 57.8 0.9
NE2 B:HIS200 2.3 27.3 1.0
C14 B:B30312 2.4 58.3 0.9
C15 B:B30312 2.6 58.9 0.9
C13 B:B30312 2.7 59.6 0.9
C12 B:B30312 2.8 58.8 0.9
N8 B:B30312 3.0 45.0 0.9
C10 B:B30312 3.2 55.1 0.9
CE1 B:HIS200 3.2 26.2 1.0
C9 B:B30312 3.3 50.0 0.9
CD2 B:HIS200 3.4 26.0 1.0
C7 B:B30312 3.8 40.9 0.9
OXD B:B30312 3.8 60.3 0.9
OXA B:B30312 3.9 59.7 0.9
O B:PRO201 4.0 25.1 1.0
C1 B:B30312 4.3 35.9 1.0
C2 B:B30312 4.3 31.5 1.0
ND1 B:HIS200 4.4 26.4 1.0
NE2 B:HIS64 4.5 19.5 1.0
CG B:HIS200 4.5 24.4 1.0
O7 B:B30312 4.6 42.5 0.9
CE1 B:HIS64 4.9 18.2 1.0
CE1 B:HIS67 4.9 22.8 1.0
CZ2 B:TRP5 4.9 24.6 1.0

Copper binding site 5 out of 6 in 2foy

Go back to Copper Binding Sites List in 2foy
Copper binding site 5 out of 6 in the Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu314

b:66.3
occ:1.00
 CU B:B30314 0.0 66.3 1.0
OXB B:B30314 2.0 67.7 1.0
OXC B:B30314 2.0 67.5 1.0
NE2 B:HIS243 2.3 22.4 1.0
N11 B:B30314 2.3 65.8 1.0
C14 B:B30314 2.4 66.9 1.0
C15 B:B30314 2.6 67.5 1.0
C13 B:B30314 2.7 68.3 1.0
N8 B:B30314 2.7 47.8 1.0
C12 B:B30314 2.8 67.0 1.0
CD2 B:HIS243 3.0 24.5 1.0
C10 B:B30314 3.1 61.2 1.0
C2 B:B30314 3.2 40.1 0.8
C9 B:B30314 3.3 54.2 1.0
C7 B:B30314 3.4 43.8 1.0
CE1 B:HIS243 3.5 24.1 1.0
C1 B:B30314 3.8 41.1 0.8
OXD B:B30314 3.8 68.9 1.0
OXA B:B30314 3.9 69.6 1.0
CG B:HIS243 4.3 21.1 1.0
OD1 B:ASP8 4.3 56.5 1.0
O7 B:B30314 4.3 41.8 1.0
C3 B:B30314 4.3 37.2 0.8
CB B:GLN242 4.4 24.3 1.0
ND1 B:HIS243 4.4 23.5 1.0
CG B:GLN242 4.9 33.5 1.0

Copper binding site 6 out of 6 in 2foy

Go back to Copper Binding Sites List in 2foy
Copper binding site 6 out of 6 in the Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Human Carbonic Anhydrase I Complexed with A Two-Prong Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu316

b:35.7
occ:1.00
 CU B:B30316 0.0 35.7 1.0
OXB B:B30316 2.0 37.9 0.6
OXC B:B30316 2.0 37.4 0.6
N11 B:B30316 2.3 36.7 0.6
NE2 B:HIS103 2.4 47.2 1.0
C14 B:B30316 2.4 36.9 0.6
C15 B:B30316 2.6 36.7 0.6
C13 B:B30316 2.7 37.6 0.6
C12 B:B30316 2.8 37.1 0.6
N8 B:B30316 3.0 39.2 0.6
CD2 B:HIS103 3.1 45.3 1.0
C10 B:B30316 3.2 37.5 0.6
C9 B:B30316 3.4 38.0 0.6
CE1 B:HIS103 3.5 47.5 1.0
OE2 B:GLU102 3.5 60.4 1.0
C7 B:B30316 3.6 39.3 0.6
OXD B:B30316 3.8 38.3 0.6
OXA B:B30316 3.9 38.6 0.6
C1 B:B30316 4.0 39.6 0.7
C2 B:B30316 4.1 39.2 0.7
CG B:HIS103 4.3 42.3 1.0
O7 B:B30316 4.4 40.7 0.6
ND1 B:HIS103 4.5 45.5 1.0
CD B:GLU102 4.6 56.2 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: Tue Jul 30 23:31:38 2024

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