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Copper in PDB 6sks: Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1)

Enzymatic activity of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1)

All present enzymatic activity of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1):
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1), PDB code: 6sks was solved by M.R.Groves, W.Wang, N.Van Oosterwijk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.30 / 1.75
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.406, 67.406, 123.319, 90.00, 90.00, 120.00
R / Rfree (%) 16.9 / 19.4

Other elements in 6sks:

The structure of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1) also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1) (pdb code 6sks). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1), PDB code: 6sks:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 6sks

Go back to Copper Binding Sites List in 6sks
Copper binding site 1 out of 4 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:33.0
occ:1.00
 NE2 A:HIS14 2.0 34.4 1.0
NE2 A:HIS2 2.0 36.6 1.0
OD2 A:ASP18 2.3 45.2 1.0
O A:HOH571 2.5 36.6 1.0
CE1 A:HIS14 2.6 35.7 1.0
CD2 A:HIS2 2.9 37.9 1.0
CE1 A:HIS2 3.1 38.4 1.0
CG A:ASP18 3.1 40.6 1.0
OD1 A:ASP18 3.2 41.6 1.0
CD2 A:HIS14 3.2 34.1 1.0
ND1 A:HIS14 3.8 35.8 1.0
CG A:HIS2 4.1 40.3 1.0
ND1 A:HIS2 4.1 38.1 1.0
CG A:HIS14 4.2 33.1 1.0
O A:HOH580 4.4 42.2 1.0
CB A:ASP18 4.6 36.9 1.0

Copper binding site 2 out of 4 in 6sks

Go back to Copper Binding Sites List in 6sks
Copper binding site 2 out of 4 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:54.1
occ:1.00
 O A:HOH538 2.4 29.8 1.0
N4 A:E68308 2.4 43.5 1.0
C13 A:E68308 2.9 46.8 1.0
O A:HOH548 3.0 51.9 1.0
C14 A:E68308 3.6 47.7 1.0
O A:HOH488 3.9 38.2 1.0
OD2 A:ASP71 4.1 32.2 1.0
C12 A:E68308 4.2 44.5 1.0
OD1 A:ASP71 4.3 33.1 1.0
N5 A:E68308 4.5 46.5 1.0
CG A:ASP71 4.6 32.4 1.0
CB A:ASP128 4.7 28.8 1.0
N A:PHE129 4.8 27.8 1.0
CB A:PHE129 5.0 28.4 1.0

Copper binding site 3 out of 4 in 6sks

Go back to Copper Binding Sites List in 6sks
Copper binding site 3 out of 4 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu303

b:37.6
occ:0.50
 CD2 A:HIS3 1.7 42.4 0.5
O A:TRP4 2.1 36.5 1.0
NE2 A:HIS63 2.2 34.8 0.5
O A:HOH575 2.5 31.7 0.5
N A:TRP4 2.5 40.8 1.0
O A:HOH401 2.5 17.7 0.5
CE1 A:HIS63 2.5 30.3 0.5
CG A:HIS3 2.6 42.4 0.5
NE2 A:HIS3 2.8 42.4 0.5
CE1 A:HIS63 2.8 35.4 0.5
C A:TRP4 2.9 34.2 1.0
C A:HIS3 3.0 43.3 0.5
C A:HIS3 3.1 45.0 0.5
CB A:HIS3 3.1 48.0 0.5
CA A:TRP4 3.1 37.8 1.0
CB A:HIS3 3.1 42.7 0.5
CD1 A:TRP4 3.2 34.1 1.0
CG A:TRP4 3.2 34.4 1.0
CD2 A:HIS63 3.4 34.6 0.5
ND1 A:HIS3 3.4 52.2 0.5
NE2 A:HIS63 3.4 31.6 0.5
NE1 A:TRP4 3.5 34.9 1.0
ND1 A:HIS63 3.5 30.2 0.5
CD2 A:TRP4 3.5 33.6 1.0
CA A:HIS3 3.5 42.5 0.5
CA A:HIS3 3.6 45.3 0.5
CE2 A:TRP4 3.7 33.2 1.0
O A:HIS3 3.7 46.0 0.5
CG A:HIS3 3.7 51.2 0.5
CU A:CU304 3.7 49.1 0.5
ND1 A:HIS3 3.7 42.8 0.5
CB A:TRP4 3.8 36.8 1.0
CE1 A:HIS3 3.8 42.7 0.5
O A:HIS3 3.9 47.5 0.5
ND1 A:HIS63 4.1 34.6 0.5
N A:GLY5 4.2 31.5 1.0
CG A:HIS63 4.3 33.6 0.5
CE3 A:TRP4 4.4 32.3 1.0
CZ2 A:TRP4 4.5 31.4 1.0
CD2 A:HIS63 4.6 31.3 0.5
CG A:HIS63 4.7 30.4 0.5
CE1 A:HIS3 4.7 54.0 0.5
CA A:GLY5 4.8 30.1 1.0
N A:HIS3 4.9 40.8 0.5
N A:HIS3 4.9 42.5 0.5

Copper binding site 4 out of 4 in 6sks

Go back to Copper Binding Sites List in 6sks
Copper binding site 4 out of 4 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu304

b:49.1
occ:0.50
 NE2 A:HIS63 1.7 31.6 0.5
CE1 A:HIS63 2.3 35.4 0.5
NE2 A:HIS3 2.4 42.4 0.5
O A:HOH553 2.4 54.0 1.0
CE1 A:HIS63 2.7 30.3 0.5
CD2 A:HIS63 2.8 31.3 0.5
CD2 A:HIS3 2.9 42.4 0.5
ND1 A:HIS63 2.9 34.6 0.5
CE1 A:HIS3 3.1 42.7 0.5
NE2 A:HIS63 3.4 34.8 0.5
O A:ASN61 3.7 38.1 1.0
CG A:HIS3 3.7 42.4 0.5
CU A:CU303 3.7 37.6 0.5
ND1 A:HIS3 3.8 42.8 0.5
ND1 A:HIS63 3.8 30.2 0.5
CG A:HIS63 3.9 30.4 0.5
ND1 A:HIS3 4.0 52.2 0.5
CG A:HIS63 4.2 33.6 0.5
O A:HOH575 4.4 31.7 0.5
CD2 A:HIS63 4.4 34.6 0.5
CE1 A:HIS3 4.5 54.0 0.5
CE A:LYS168 4.6 48.4 1.0
O A:HOH563 4.7 44.1 1.0
NE1 A:TRP4 4.7 34.9 1.0
CG A:HIS3 4.7 51.2 0.5
C A:ASN61 4.9 35.4 1.0
CB A:HIS3 4.9 42.7 0.5
CE2 A:TRP4 5.0 33.2 1.0
CB A:HIS3 5.0 48.0 0.5

Reference:

M.R.Groves, W.Wang, N.Van Oosterwijk, M.Witte, J.Lohse. Target Diazotransfer Reagents to Label Metalloenzymes To Be Published.
Page generated: Sun Dec 13 11:25:52 2020

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