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Copper in PDB 6skv: Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2)

Enzymatic activity of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2)

All present enzymatic activity of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2):
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2), PDB code: 6skv 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 (°) 67.308, 67.308, 122.948, 90.00, 90.00, 120.00
R / Rfree (%) 17.1 / 18.9

Other elements in 6skv:

The structure of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2) 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 (SH2) (pdb code 6skv). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2), PDB code: 6skv:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 6skv

Go back to Copper Binding Sites List in 6skv
Copper binding site 1 out of 3 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2)


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 (SH2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:37.6
occ:1.00
 NE2 A:HIS3 2.0 45.0 1.0
OD2 A:ASP19 2.3 48.8 1.0
CE1 A:HIS15 2.3 39.9 1.0
O A:HOH1101 2.3 26.0 0.5
NE2 A:HIS15 2.4 38.7 1.0
CD2 A:HIS3 2.9 45.9 1.0
CE1 A:HIS3 3.1 46.3 1.0
CG A:ASP19 3.1 44.7 1.0
OD1 A:ASP19 3.2 44.4 1.0
ND1 A:HIS15 3.6 41.9 1.0
CD2 A:HIS15 3.7 40.2 1.0
O A:HIS4 3.8 60.4 1.0
CG A:HIS3 4.1 50.1 1.0
ND1 A:HIS3 4.1 47.4 1.0
O A:HOH1227 4.2 28.4 0.5
CG A:HIS15 4.3 38.2 1.0
CB A:ASP19 4.6 41.7 1.0

Copper binding site 2 out of 3 in 6skv

Go back to Copper Binding Sites List in 6skv
Copper binding site 2 out of 3 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2)


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 (SH2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1002

b:42.9
occ:0.50
 NE2 A:HIS64 2.2 46.0 1.0
ND1 A:HIS4 2.2 67.3 1.0
O A:TRP5 2.3 44.5 1.0
CU A:CU1003 2.5 45.8 0.5
N A:TRP5 2.7 52.1 1.0
CG A:HIS4 2.9 62.9 1.0
CB A:HIS4 2.9 59.7 1.0
CD2 A:HIS64 3.1 46.0 1.0
CE1 A:HIS64 3.2 50.4 1.0
C A:TRP5 3.3 41.9 1.0
CE1 A:HIS4 3.3 66.9 1.0
CD1 A:TRP5 3.5 42.5 1.0
NE1 A:TRP5 3.5 40.5 1.0
CG A:TRP5 3.5 41.1 1.0
CD2 A:TRP5 3.6 39.0 1.0
CA A:TRP5 3.6 45.9 1.0
CE2 A:TRP5 3.6 40.1 1.0
C A:HIS4 3.7 57.6 1.0
CA A:HIS4 3.8 56.6 1.0
CD2 A:HIS4 4.1 65.5 1.0
CB A:TRP5 4.2 43.5 1.0
CG A:HIS64 4.3 43.7 1.0
NE2 A:HIS4 4.3 67.9 1.0
ND1 A:HIS64 4.3 49.5 1.0
O A:HOH1124 4.3 49.3 1.0
CE3 A:TRP5 4.3 38.0 1.0
CZ2 A:TRP5 4.3 37.3 1.0
N A:GLY6 4.4 36.9 1.0
O A:HOH1230 4.7 62.4 1.0
N A:HIS4 4.8 52.1 1.0
O A:HIS4 4.8 60.4 1.0
CA A:GLY6 4.9 34.7 1.0
CZ3 A:TRP5 4.9 36.6 1.0
CH2 A:TRP5 4.9 37.5 1.0

Copper binding site 3 out of 3 in 6skv

Go back to Copper Binding Sites List in 6skv
Copper binding site 3 out of 3 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH2)


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 (SH2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1003

b:45.8
occ:0.50
 O A:TRP5 2.0 44.5 1.0
CU A:CU1002 2.5 42.9 0.5
O A:HOH1124 2.9 49.3 1.0
NE2 A:HIS64 3.0 46.0 1.0
C A:TRP5 3.1 41.9 1.0
CD2 A:HIS64 3.2 46.0 1.0
O A:HOH1233 3.5 52.4 1.0
CA A:GLY6 3.7 34.7 1.0
N A:GLY6 3.9 36.9 1.0
N A:TRP5 3.9 52.1 1.0
O A:GLY63 4.1 35.2 1.0
CE1 A:HIS64 4.1 50.4 1.0
O A:HOH1230 4.2 62.4 1.0
CA A:TRP5 4.2 45.9 1.0
ND2 A:ASN11 4.2 39.2 1.0
CB A:HIS4 4.4 59.7 1.0
CG A:HIS64 4.4 43.7 1.0
ND1 A:HIS4 4.4 67.3 1.0
O A:HOH1234 4.7 41.6 1.0
ND1 A:HIS64 4.8 49.5 1.0
C A:HIS4 4.8 57.6 1.0
CG A:HIS4 4.9 62.9 1.0
CD2 A:TRP5 5.0 39.0 1.0

Reference:

M.R.Groves, W.Wang, N.Van Oosterwijk, M.Witte, J.Lohse. Target Diazotransfer Reagents to Label Metalloenzymes To Be Published.
Page generated: Wed Jul 31 07:30:19 2024

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