Atomistry » Zinc » PDB 6s6y-6sdi » 6scp
Atomistry »
  Zinc »
    PDB 6s6y-6sdi »
      6scp »

Zinc in PDB 6scp: Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz

Protein crystallography data

The structure of Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz, PDB code: 6scp was solved by A.Sogues, A.M.Wehenkel, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.53 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 35.322, 53.079, 95.629, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 21.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz (pdb code 6scp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz, PDB code: 6scp:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 6scp

Go back to Zinc Binding Sites List in 6scp
Zinc binding site 1 out of 6 in the Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:18.9
occ:0.74
OE2 A:GLU78 1.9 25.5 1.0
OD1 A:ASP79 2.0 27.2 1.0
O A:HOH308 2.1 28.3 1.0
CD A:GLU78 2.9 43.7 1.0
CG A:ASP79 3.0 26.1 1.0
CG A:GLU78 3.2 32.6 1.0
OD2 A:ASP79 3.4 25.3 1.0
O A:HOH302 4.0 24.9 1.0
OE1 A:GLU78 4.0 32.8 1.0
OG A:SER76 4.2 28.0 1.0
CB A:ASP79 4.4 20.9 1.0
N A:ASP79 4.5 20.9 1.0
O A:HOH346 4.6 32.1 1.0
ND1 A:HIS75 4.6 22.1 1.0
CB A:GLU78 4.6 25.1 1.0
CA A:ASP79 4.7 20.2 1.0
C A:GLU78 4.8 25.9 1.0
CB A:HIS75 4.8 19.3 1.0

Zinc binding site 2 out of 6 in 6scp

Go back to Zinc Binding Sites List in 6scp
Zinc binding site 2 out of 6 in the Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:31.1
occ:0.43
O A:HOH319 1.9 31.4 0.5
N A:MET63 2.1 53.3 1.0
O A:HOH319 2.6 30.6 0.5
CA A:MET63 3.3 52.7 1.0
O A:MET63 4.2 50.6 1.0
C A:MET63 4.2 51.9 1.0
CG A:MET63 4.3 60.6 1.0
CB A:MET63 4.4 55.8 1.0
O A:SER67 4.5 29.2 1.0
OG1 A:THR68 4.9 26.5 1.0

Zinc binding site 3 out of 6 in 6scp

Go back to Zinc Binding Sites List in 6scp
Zinc binding site 3 out of 6 in the Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:18.6
occ:0.60
O B:HOH310 1.9 34.8 1.0
O B:HOH301 2.0 41.2 1.0
O B:HOH323 2.2 34.8 1.0
O B:HOH352 3.8 46.8 1.0
OE2 B:GLU104 4.0 25.6 1.0
OE1 B:GLU104 4.1 20.9 1.0
O B:HIS75 4.1 20.9 1.0
CD B:GLU104 4.4 31.7 1.0

Zinc binding site 4 out of 6 in 6scp

Go back to Zinc Binding Sites List in 6scp
Zinc binding site 4 out of 6 in the Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn202

b:19.9
occ:0.87
ND1 B:HIS75 1.9 24.6 1.0
O B:HOH302 2.2 25.8 1.0
CE1 B:HIS75 2.9 24.9 1.0
CG B:HIS75 3.0 23.6 1.0
CB B:HIS75 3.4 20.0 1.0
O B:HOH303 3.9 29.8 1.0
N B:HIS75 4.0 19.0 1.0
NE2 B:HIS75 4.0 26.0 1.0
OD2 B:ASP79 4.1 33.1 1.0
OD1 B:ASP79 4.1 38.2 1.0
CD2 B:HIS75 4.1 25.8 1.0
O B:GLU73 4.3 24.1 1.0
CA B:HIS75 4.3 19.1 1.0
CG B:ASP79 4.5 35.0 1.0
C B:LEU74 4.8 22.9 1.0

Zinc binding site 5 out of 6 in 6scp

Go back to Zinc Binding Sites List in 6scp
Zinc binding site 5 out of 6 in the Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn203

b:20.6
occ:0.86
OD1 B:ASP91 2.0 22.9 1.0
O B:GLN66 2.1 32.1 1.0
CG B:ASP91 2.7 24.8 1.0
OD2 B:ASP91 2.8 25.5 1.0
C B:GLN66 3.0 35.5 1.0
CA B:SER67 3.5 33.5 1.0
N B:SER67 3.6 33.9 1.0
C B:SER67 3.9 37.0 1.0
N B:THR68 4.0 31.1 1.0
CA B:GLN66 4.1 30.4 1.0
CB B:ASP91 4.1 23.6 1.0
CG2 B:THR68 4.3 26.1 1.0
CB B:GLN66 4.4 30.9 1.0
O B:ASP89 4.6 26.3 1.0
O B:SER67 4.6 37.2 1.0
O B:HOH317 4.6 34.3 1.0
CA B:ASP91 4.7 22.0 1.0
N B:ASP91 4.7 21.3 1.0
CB B:THR68 4.8 35.0 1.0
CB B:SER67 4.9 37.9 1.0

Zinc binding site 6 out of 6 in 6scp

Go back to Zinc Binding Sites List in 6scp
Zinc binding site 6 out of 6 in the Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn204

b:24.9
occ:0.40
O B:HOH317 2.0 34.3 1.0
N B:MET63 2.1 42.0 1.0
O B:MET63 2.3 39.7 1.0
O B:HOH343 2.6 52.3 1.0
C B:MET63 2.9 42.1 1.0
CA B:MET63 2.9 42.4 1.0
O B:SER67 3.6 37.2 1.0
O B:HOH321 3.8 31.8 1.0
N B:SER64 4.1 37.5 1.0
CB B:MET63 4.3 45.8 1.0
C B:SER67 4.7 37.0 1.0
N B:SER67 4.7 33.9 1.0
CA B:SER64 5.0 37.1 1.0

Reference:

A.Sogues, A.M.Wehenkel, P.M.Alzari. Cell Division Protein Sepf in Complex with C-Terminal Domain of Ftsz To Be Published.
Page generated: Tue Oct 29 07:13:49 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy