Atomistry » Copper » PDB 6ri2-6vbt » 6skv
Atomistry »
  Copper »
    PDB 6ri2-6vbt »
      6skv »

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy