Atomistry » Copper » PDB 6ri0-6vbs » 6skt
Atomistry »
  Copper »
    PDB 6ri0-6vbs »
      6skt »

Copper in PDB 6skt: Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0)

Enzymatic activity of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0)

All present enzymatic activity of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0):
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0), PDB code: 6skt 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) 42.40 / 1.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.619, 67.619, 123.429, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 20.4

Other elements in 6skt:

The structure of Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0) 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 (SH0) (pdb code 6skt). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0), PDB code: 6skt:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 6skt

Go back to Copper Binding Sites List in 6skt
Copper binding site 1 out of 2 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0)


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 (SH0) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:42.7
occ:1.00
ND1 A:HIS4 2.1 53.6 1.0
NE2 A:HIS15 2.1 39.7 1.0
OD2 A:ASP19 2.2 52.2 1.0
O A:HIS4 2.5 49.5 1.0
CE1 A:HIS15 3.0 39.5 1.0
CE1 A:HIS4 3.1 54.2 1.0
CG A:ASP19 3.1 52.4 1.0
CG A:HIS4 3.1 55.1 1.0
OD1 A:ASP19 3.2 54.2 1.0
CD2 A:HIS15 3.2 39.9 1.0
CB A:HIS4 3.4 55.0 1.0
C A:HIS4 3.5 51.4 1.0
CA A:HIS4 4.0 54.9 1.0
NE2 A:HIS4 4.2 56.0 1.0
ND1 A:HIS15 4.2 38.6 1.0
CD2 A:HIS4 4.2 55.6 1.0
CG A:HIS15 4.3 38.7 1.0
N A:TRP5 4.5 47.5 1.0
CB A:ASP19 4.5 49.5 1.0
CA A:TRP5 4.9 45.1 1.0
N A:HIS4 5.0 59.8 1.0

Copper binding site 2 out of 2 in 6skt

Go back to Copper Binding Sites List in 6skt
Copper binding site 2 out of 2 in the Crystal Structure of Bovine Carbonic Anhydrase II in Complex with A Benzenesulfonamide-Based Ligand (SH0)


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 (SH0) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1005

b:65.8
occ:1.00
NE2 A:HIS3 2.3 67.1 1.0
NE2 A:HIS64 2.4 55.2 1.0
O A:TRP5 2.5 43.5 1.0
O A:HOH1130 2.8 48.9 1.0
CD2 A:HIS64 2.9 53.4 1.0
CE1 A:HIS3 3.2 66.4 1.0
CD2 A:HIS3 3.3 67.9 1.0
CE1 A:HIS64 3.6 54.7 1.0
C A:TRP5 3.6 43.0 1.0
CA A:GLY6 3.9 38.6 1.0
O A:GLY63 4.2 39.6 1.0
CG A:HIS64 4.2 49.6 1.0
N A:GLY6 4.2 40.1 1.0
ND1 A:HIS3 4.3 69.0 1.0
CG A:HIS3 4.4 69.3 1.0
ND1 A:HIS64 4.5 53.0 1.0
ND2 A:ASN11 4.5 41.3 1.0
O A:HOH1226 4.5 46.8 1.0
CA A:TRP5 4.8 45.1 1.0
N A:TRP5 4.9 47.5 1.0
CD2 A:TRP5 5.0 42.0 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 07:30:17 2024

Last articles

Zn in 7WTZ
Zn in 7WTX
Zn in 7WTW
Zn in 7WT5
Zn in 7WTU
Zn in 7WTV
Zn in 7WTT
Zn in 7WT4
Zn in 7WT3
Zn in 7WSS
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy