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Zinc in PDB 1z6r: Crystal Structure of Mlc From Escherichia Coli

Protein crystallography data

The structure of Crystal Structure of Mlc From Escherichia Coli, PDB code: 1z6r was solved by A.Schiefner, K.Gerber, S.Seitz, W.Welte, K.Diederichs, W.Boos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 2.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 235.950, 74.710, 154.950, 90.00, 129.15, 90.00
R / Rfree (%) 20.3 / 26.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Mlc From Escherichia Coli (pdb code 1z6r). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Mlc From Escherichia Coli, PDB code: 1z6r:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1z6r

Go back to Zinc Binding Sites List in 1z6r
Zinc binding site 1 out of 4 in the Crystal Structure of Mlc From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Mlc From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:55.8
occ:1.00
ND1 A:HIS247 2.0 68.0 1.0
SG A:CYS264 2.2 72.0 1.0
SG A:CYS259 2.2 69.9 1.0
SG A:CYS257 2.3 73.4 1.0
CE1 A:HIS247 2.8 69.7 1.0
CB A:CYS259 3.1 70.8 1.0
CG A:HIS247 3.1 69.2 1.0
CB A:CYS257 3.2 72.8 1.0
CB A:CYS264 3.3 69.1 1.0
CB A:HIS247 3.6 68.2 1.0
CA A:HIS247 3.9 68.6 1.0
NE2 A:HIS247 4.0 71.3 1.0
CD2 A:HIS247 4.1 70.6 1.0
CA A:CYS259 4.2 70.8 1.0
N A:CYS259 4.2 71.1 1.0
O A:HIS247 4.6 68.4 1.0
CA A:CYS257 4.6 72.9 1.0
CA A:CYS264 4.7 69.3 1.0
C A:HIS247 4.7 68.7 1.0
O A:GLY246 4.8 70.2 1.0
N A:HIS247 4.9 69.2 1.0
C A:CYS257 5.0 72.9 1.0
C A:CYS259 5.0 70.5 1.0

Zinc binding site 2 out of 4 in 1z6r

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Zinc binding site 2 out of 4 in the Crystal Structure of Mlc From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Mlc From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn502

b:46.5
occ:1.00
ND1 B:HIS247 2.0 70.1 1.0
SG B:CYS259 2.1 64.2 1.0
SG B:CYS257 2.2 67.3 1.0
SG B:CYS264 2.2 70.3 1.0
CE1 B:HIS247 3.0 67.9 1.0
CG B:HIS247 3.0 67.3 1.0
CB B:CYS257 3.1 68.8 1.0
CB B:CYS259 3.1 67.4 1.0
CB B:CYS264 3.3 70.3 1.0
CB B:HIS247 3.4 67.7 1.0
CA B:HIS247 3.8 68.0 1.0
NE2 B:HIS247 4.1 67.8 1.0
CD2 B:HIS247 4.1 66.4 1.0
N B:CYS259 4.1 67.7 1.0
CA B:CYS259 4.2 67.1 1.0
CA B:CYS257 4.5 68.7 1.0
CA B:CYS264 4.7 70.0 1.0
N B:HIS247 4.7 69.4 1.0
C B:CYS257 4.8 68.5 1.0
O B:GLY246 4.8 70.6 1.0
CB B:ASN261 4.8 67.5 1.0
C B:HIS247 4.8 67.7 1.0
O B:HIS247 4.9 67.4 1.0
N B:TYR258 4.9 67.9 1.0
C B:CYS259 5.0 67.6 1.0

Zinc binding site 3 out of 4 in 1z6r

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Zinc binding site 3 out of 4 in the Crystal Structure of Mlc From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Mlc From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn503

b:71.7
occ:1.00
ND1 C:HIS247 2.0 69.3 1.0
SG C:CYS259 2.1 67.8 1.0
SG C:CYS264 2.2 72.9 1.0
SG C:CYS257 2.4 74.1 1.0
CE1 C:HIS247 2.9 70.8 1.0
CB C:CYS259 3.1 70.3 1.0
CG C:HIS247 3.1 68.4 1.0
CB C:CYS257 3.2 72.0 1.0
CB C:CYS264 3.3 71.0 1.0
CB C:HIS247 3.6 67.3 1.0
NE2 C:HIS247 4.0 71.2 1.0
CA C:HIS247 4.0 67.3 1.0
CD2 C:HIS247 4.1 68.8 1.0
CA C:CYS259 4.2 69.7 1.0
N C:CYS259 4.2 70.2 1.0
CA C:CYS257 4.6 72.0 1.0
O C:GLY246 4.6 67.8 1.0
CA C:CYS264 4.7 70.6 1.0
C C:CYS257 4.8 71.2 1.0
C C:CYS259 4.9 69.8 1.0
C C:HIS247 4.9 67.0 1.0
O C:HIS247 5.0 66.8 1.0
N C:HIS247 5.0 67.5 1.0

Zinc binding site 4 out of 4 in 1z6r

Go back to Zinc Binding Sites List in 1z6r
Zinc binding site 4 out of 4 in the Crystal Structure of Mlc From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Mlc From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn504

b:87.0
occ:1.00
ND1 D:HIS247 2.3 71.8 1.0
SG D:CYS264 2.5 78.3 1.0
SG D:CYS259 2.5 80.0 1.0
SG D:CYS257 2.6 80.1 1.0
CB D:CYS259 3.1 77.4 1.0
CB D:CYS257 3.2 78.5 1.0
CG D:HIS247 3.2 71.1 1.0
CE1 D:HIS247 3.2 71.5 1.0
CB D:CYS264 3.3 75.1 1.0
CB D:HIS247 3.4 70.1 1.0
CA D:HIS247 3.7 70.1 1.0
N D:CYS259 4.2 77.1 1.0
CA D:CYS259 4.2 77.2 1.0
CD2 D:HIS247 4.3 71.7 1.0
NE2 D:HIS247 4.3 71.7 1.0
O D:HIS247 4.4 69.7 1.0
C D:HIS247 4.5 70.1 1.0
CA D:CYS257 4.6 78.4 1.0
CA D:CYS264 4.8 75.2 1.0
O D:GLY246 4.8 71.5 1.0
N D:HIS247 4.8 70.3 1.0
C D:CYS257 4.8 78.0 1.0
N D:TYR258 5.0 77.6 1.0

Reference:

A.Schiefner, K.Gerber, S.Seitz, W.Welte, K.Diederichs, W.Boos. The Crystal Structure of Mlc, A Global Regulator of Sugar Metabolism in Escherichia Coli J.Biol.Chem. V. 280 29073 2005.
ISSN: ISSN 0021-9258
PubMed: 15929984
DOI: 10.1074/JBC.M504215200
Page generated: Wed Oct 16 21:07:41 2024

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