Atomistry » Copper » PDB 1rju-1tl4 » 1t16
Atomistry »
  Copper »
    PDB 1rju-1tl4 »
      1t16 »

Copper in PDB 1t16: Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli

Protein crystallography data

The structure of Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli, PDB code: 1t16 was solved by B.Van Den Berg, P.N.Black, W.M.Clemons Jr., T.A.Rapoport, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 100.380, 68.664, 106.024, 90.00, 96.37, 90.00
R / Rfree (%) 25.7 / 30.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli (pdb code 1t16). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli, PDB code: 1t16:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 1t16

Go back to Copper Binding Sites List in 1t16
Copper binding site 1 out of 6 in the Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli


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 the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu428

b:90.8
occ:1.00
NE2 A:HIS423 2.1 92.0 1.0
NE2 A:HIS426 2.2 80.7 1.0
CE1 A:HIS423 2.5 92.2 1.0
CD2 A:HIS426 2.9 81.8 1.0
CE1 A:HIS426 3.2 81.4 1.0
CD2 A:HIS423 3.2 93.5 1.0
OD2 A:ASP90 3.4 0.7 1.0
ND1 A:HIS423 3.6 93.0 1.0
CG A:HIS423 4.0 92.7 1.0
CG A:HIS426 4.0 82.2 1.0
ND1 A:HIS426 4.2 82.3 1.0
CG A:ASP90 4.4 0.7 1.0
O A:ASP41 4.4 77.5 1.0
O A:HIS424 4.6 92.2 1.0
OD1 A:ASP90 4.7 0.4 1.0

Copper binding site 2 out of 6 in 1t16

Go back to Copper Binding Sites List in 1t16
Copper binding site 2 out of 6 in the Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli


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 the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu429

b:67.8
occ:1.00
ND1 A:HIS424 1.9 94.4 1.0
O A:HOH509 2.2 67.9 1.0
CE1 A:HIS422 2.3 99.1 1.0
CE1 A:HIS424 2.9 94.2 1.0
NE2 A:HIS422 2.9 99.7 1.0
CG A:HIS424 2.9 93.4 1.0
CA A:HIS424 3.3 92.6 1.0
CB A:HIS424 3.3 93.0 1.0
ND1 A:HIS422 3.4 98.5 1.0
NE2 A:HIS424 4.0 93.5 1.0
CD2 A:HIS424 4.0 93.4 1.0
N A:HIS425 4.1 95.8 1.0
N A:HIS424 4.2 92.5 1.0
CD2 A:HIS422 4.2 99.5 1.0
C A:HIS424 4.3 93.9 1.0
CG A:HIS422 4.4 98.0 1.0
O A:HIS423 4.6 90.4 1.0
C A:HIS423 4.7 91.8 1.0

Copper binding site 3 out of 6 in 1t16

Go back to Copper Binding Sites List in 1t16
Copper binding site 3 out of 6 in the Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli


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 the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu430

b:84.6
occ:1.00
NE2 A:HIS425 2.0 0.9 1.0
NE2 A:HIS427 2.6 82.8 1.0
CD2 A:HIS427 2.6 81.9 1.0
CD2 A:HIS425 2.8 0.8 1.0
CE1 A:HIS425 3.1 0.9 1.0
CE1 A:HIS427 3.6 82.3 1.0
CG A:HIS427 3.7 80.7 1.0
CG A:HIS425 4.0 0.4 1.0
ND1 A:HIS425 4.1 0.3 1.0
ND1 A:HIS427 4.2 82.0 1.0
CB A:HIS427 4.8 78.4 1.0

Copper binding site 4 out of 6 in 1t16

Go back to Copper Binding Sites List in 1t16
Copper binding site 4 out of 6 in the Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli


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 the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu428

b:92.5
occ:1.00
CD2 B:HIS423 3.5 0.3 1.0
CB B:HIS426 3.6 0.8 1.0
CG B:HIS426 4.0 0.8 1.0
O B:HIS424 4.2 0.0 1.0
NE2 B:HIS423 4.2 1.0 1.0
CG B:HIS423 4.5 0.4 1.0
O B:ASP41 4.5 97.8 1.0
CD2 B:HIS426 4.6 0.1 1.0
ND1 B:HIS426 4.6 0.4 1.0
OD2 B:ASP90 4.8 0.7 1.0
CA B:HIS426 4.8 0.8 1.0
N B:HIS426 4.9 0.8 1.0
CB B:HIS423 5.0 0.3 1.0
O B:HOH441 5.0 48.0 1.0

Copper binding site 5 out of 6 in 1t16

Go back to Copper Binding Sites List in 1t16
Copper binding site 5 out of 6 in the Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu429

b:78.3
occ:1.00
NE2 B:HIS424 2.5 0.2 1.0
CE1 B:HIS422 2.5 0.5 1.0
NE2 B:HIS422 3.2 0.3 1.0
CD2 B:HIS424 3.3 0.9 1.0
CE1 B:HIS424 3.5 0.7 1.0
ND1 B:HIS422 3.6 0.8 1.0
CD2 B:HIS422 4.5 0.8 1.0
CG B:HIS424 4.5 0.6 1.0
ND1 B:HIS424 4.6 0.8 1.0
CG B:HIS422 4.7 0.2 1.0

Copper binding site 6 out of 6 in 1t16

Go back to Copper Binding Sites List in 1t16
Copper binding site 6 out of 6 in the Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of the Bacterial Fatty Acid Transporter Fadl From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu430

b:0.9
occ:1.00
CE1 B:HIS425 2.2 0.0 1.0
NE2 B:HIS425 2.7 0.9 1.0
ND1 B:HIS425 3.4 0.3 1.0
ND1 B:HIS427 3.8 0.1 1.0
CE1 B:HIS427 4.0 1.0 1.0
CD2 B:HIS425 4.1 0.4 1.0
CG B:HIS425 4.4 0.8 1.0
O B:HIS426 4.6 0.5 1.0
CG B:HIS427 5.0 0.4 1.0

Reference:

B.Van Den Berg, P.N.Black, W.M.Clemons Jr., T.A.Rapoport. Crystal Structure of the Long-Chain Fatty Acid Transporter Fadl. Science V. 304 1506 2004.
ISSN: ISSN 0036-8075
PubMed: 15178802
DOI: 10.1126/SCIENCE.1097524
Page generated: Sun Dec 13 11:02:07 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy