Atomistry » Copper » PDB 1x9r-2ahl » 1xtl
Atomistry »
  Copper »
    PDB 1x9r-2ahl »
      1xtl »

Copper in PDB 1xtl: Crystal Structure of P104H Mutant of Sod-Like Protein From Bacillus Subtilis.

Protein crystallography data

The structure of Crystal Structure of P104H Mutant of Sod-Like Protein From Bacillus Subtilis., PDB code: 1xtl was solved by V.Calderone, S.Mangani, L.Banci, M.Benvenuti, I.Bertini, M.S.Viezzoli, A.Fantoni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.92 / 2.00
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 52.147, 56.586, 59.118, 78.24, 89.91, 85.47
R / Rfree (%) 23.2 / 29.9

Other elements in 1xtl:

The structure of Crystal Structure of P104H Mutant of Sod-Like Protein From Bacillus Subtilis. also contains other interesting chemical elements:

Zinc (Zn) 10 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of P104H Mutant of Sod-Like Protein From Bacillus Subtilis. (pdb code 1xtl). 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 P104H Mutant of Sod-Like Protein From Bacillus Subtilis., PDB code: 1xtl:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1xtl

Go back to Copper Binding Sites List in 1xtl
Copper binding site 1 out of 4 in the Crystal Structure of P104H Mutant of Sod-Like Protein From Bacillus Subtilis.


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 P104H Mutant of Sod-Like Protein From Bacillus Subtilis. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1171

b:27.7
occ:1.00
NE2 B:HIS104 2.0 7.5 1.0
NE2 B:HIS166 2.2 6.0 1.0
CD2 B:HIS86 2.5 22.2 1.0
OH B:TYR88 2.7 22.2 1.0
CE1 B:HIS104 2.9 20.2 1.0
CD2 B:HIS166 2.9 14.2 1.0
CD2 B:HIS104 3.1 17.5 1.0
NE2 B:HIS86 3.2 20.8 1.0
CG B:HIS86 3.3 20.5 1.0
CE1 B:HIS166 3.4 17.5 1.0
CZ B:TYR88 3.4 23.0 1.0
CE1 B:TYR88 3.5 27.6 1.0
CB B:HIS86 3.9 19.2 1.0
CB B:SER177 3.9 23.2 1.0
ND1 B:HIS104 4.0 20.1 1.0
CE1 B:HIS86 4.1 22.2 1.0
CG B:HIS166 4.2 16.4 1.0
ND1 B:HIS86 4.2 21.1 1.0
CG B:HIS104 4.2 13.3 1.0
ND1 B:HIS166 4.3 10.4 1.0
CE2 B:TYR88 4.6 23.6 1.0
CD1 B:TYR88 4.7 25.1 1.0
O B:SER177 4.8 23.7 1.0
CA B:SER177 4.8 24.0 1.0
OG B:SER177 4.8 28.2 1.0

Copper binding site 2 out of 4 in 1xtl

Go back to Copper Binding Sites List in 1xtl
Copper binding site 2 out of 4 in the Crystal Structure of P104H Mutant of Sod-Like Protein From Bacillus Subtilis.


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 P104H Mutant of Sod-Like Protein From Bacillus Subtilis. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1173

b:27.9
occ:1.00
NE2 A:HIS166 2.1 3.9 1.0
NE2 A:HIS104 2.1 11.5 1.0
ND1 A:HIS86 2.2 26.0 1.0
OH A:TYR88 2.7 24.4 1.0
CD2 A:HIS166 2.9 17.0 1.0
CE1 A:HIS86 3.0 24.1 1.0
CG A:HIS86 3.1 20.4 1.0
CD2 A:HIS104 3.1 16.5 1.0
CE1 A:HIS166 3.1 13.3 1.0
CE1 A:HIS104 3.1 17.1 1.0
CE2 A:TYR88 3.2 24.6 1.0
CZ A:TYR88 3.4 20.3 1.0
CB A:HIS86 3.5 19.6 1.0
CB A:SER177 3.8 24.2 1.0
NE2 A:HIS86 4.0 22.8 1.0
CD2 A:HIS86 4.0 22.0 1.0
CG A:HIS166 4.1 14.0 1.0
ND1 A:HIS166 4.2 6.8 1.0
CG A:HIS104 4.2 19.5 1.0
ND1 A:HIS104 4.2 20.9 1.0
CD2 A:TYR88 4.5 20.6 1.0
CE1 A:TYR88 4.6 20.8 1.0
O A:SER177 4.7 25.5 1.0
CA A:SER177 4.7 24.6 1.0
OG A:SER177 4.9 28.3 1.0
CA A:HIS86 4.9 19.7 1.0
O A:HOH1397 4.9 28.9 1.0

Copper binding site 3 out of 4 in 1xtl

Go back to Copper Binding Sites List in 1xtl
Copper binding site 3 out of 4 in the Crystal Structure of P104H Mutant of Sod-Like Protein From Bacillus Subtilis.


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 P104H Mutant of Sod-Like Protein From Bacillus Subtilis. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu1175

b:34.5
occ:1.00
NE2 C:HIS104 1.9 11.6 1.0
NE2 C:HIS166 2.2 16.5 1.0
OH C:TYR88 2.3 21.1 1.0
ND1 C:HIS86 2.5 25.6 1.0
CE1 C:HIS104 2.8 11.2 1.0
CE1 C:HIS166 2.9 21.1 1.0
CD2 C:HIS104 3.0 15.2 1.0
CE1 C:HIS86 3.0 16.6 1.0
CZ C:TYR88 3.1 18.9 1.0
CD2 C:HIS166 3.1 19.6 1.0
CE1 C:TYR88 3.2 17.3 1.0
CG C:HIS86 3.3 19.4 1.0
O C:HOH1361 3.7 22.6 1.0
NE2 C:HIS86 3.9 19.7 1.0
ND1 C:HIS104 3.9 6.9 1.0
CB C:HIS86 3.9 20.4 1.0
ND1 C:HIS166 4.0 21.0 1.0
CB C:SER177 4.0 27.6 1.0
CG C:HIS104 4.0 13.7 1.0
CD2 C:HIS86 4.0 18.1 1.0
CG C:HIS166 4.1 22.3 1.0
CE2 C:TYR88 4.3 11.4 1.0
CD1 C:TYR88 4.5 17.1 1.0
O C:SER177 4.8 27.0 1.0
OG C:SER180 4.8 25.3 1.0
CA C:SER177 4.9 26.8 1.0
OG C:SER177 5.0 32.8 1.0

Copper binding site 4 out of 4 in 1xtl

Go back to Copper Binding Sites List in 1xtl
Copper binding site 4 out of 4 in the Crystal Structure of P104H Mutant of Sod-Like Protein From Bacillus Subtilis.


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 P104H Mutant of Sod-Like Protein From Bacillus Subtilis. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu1177

b:29.0
occ:1.00
NE2 D:HIS104 2.0 2.0 1.0
NE2 D:HIS166 2.1 5.3 1.0
OH D:TYR88 2.2 20.5 1.0
ND1 D:HIS86 2.4 28.4 1.0
CE1 D:HIS166 2.7 7.0 1.0
CD2 D:HIS166 2.7 16.4 1.0
CD2 D:HIS104 2.9 14.9 1.0
CZ D:TYR88 3.0 16.0 1.0
CE1 D:TYR88 3.1 7.4 1.0
CE1 D:HIS104 3.1 20.6 1.0
CE1 D:HIS86 3.2 29.1 1.0
ND1 D:HIS166 3.5 21.3 1.0
CG D:HIS86 3.6 20.4 1.0
CG D:HIS166 3.6 17.6 1.0
O D:HOH1383 4.0 21.7 1.0
CB D:HIS86 4.0 17.0 1.0
CB D:SER177 4.0 27.9 1.0
CG D:HIS104 4.1 4.3 1.0
ND1 D:HIS104 4.2 2.0 1.0
CE2 D:TYR88 4.3 15.2 1.0
NE2 D:HIS86 4.4 24.1 1.0
CD1 D:TYR88 4.5 10.8 1.0
CD2 D:HIS86 4.6 26.5 1.0
O D:HOH1370 4.6 20.1 1.0
OG D:SER180 4.8 23.5 1.0
CG2 D:ILE164 4.9 17.2 1.0
O D:SER177 4.9 28.2 1.0
OG D:SER177 5.0 26.6 1.0
CB D:HIS166 5.0 23.2 1.0
CA D:SER177 5.0 27.1 1.0

Reference:

L.Banci, M.Benvenuti, I.Bertini, D.E.Cabelli, V.Calderone, A.Fantoni, S.Mangani, M.Migliardi, M.S.Viezzoli. From An Inactive Prokaryotic Sod Homologue to An Active Protein Through Site-Directed Mutagenesis. J.Am.Chem.Soc. V. 127 13287 2005.
ISSN: ISSN 0002-7863
PubMed: 16173759
DOI: 10.1021/JA052790O
Page generated: Sun Dec 13 11:03:02 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy