Atomistry » Zinc » PDB 3phx-3ptm » 3pnz
Atomistry »
  Zinc »
    PDB 3phx-3ptm »
      3pnz »

Zinc in PDB 3pnz: Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes

Protein crystallography data

The structure of Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes, PDB code: 3pnz was solved by A.A.Fedorov, E.V.Fedorov, D.F.Xiang, F.M.Raushel, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.58 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 152.723, 62.933, 152.744, 90.00, 89.97, 90.00
R / Rfree (%) 17.8 / 19.8

Zinc Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Zinc atom in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes (pdb code 3pnz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 12 binding sites of Zinc where determined in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes, PDB code: 3pnz:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 1 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


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 the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn333

b:26.5
occ:0.63
O3 A:PO4335 2.0 25.3 1.0
NE2 A:HIS24 2.1 21.8 1.0
NE2 A:HIS22 2.1 20.4 1.0
OQ1 A:KCX154 2.3 25.1 0.9
OD1 A:ASP272 2.5 23.7 1.0
CE1 A:HIS24 3.1 24.2 1.0
CD2 A:HIS22 3.1 21.8 1.0
CD2 A:HIS24 3.1 20.5 1.0
P A:PO4335 3.1 29.6 0.5
CE1 A:HIS22 3.1 23.9 1.0
O1 A:PO4335 3.2 27.9 0.5
CG A:ASP272 3.3 23.7 1.0
CX A:KCX154 3.3 22.9 0.4
OD2 A:ASP272 3.5 26.7 1.0
OQ2 A:KCX154 3.7 22.3 0.6
ZN A:ZN334 3.8 25.3 0.4
O2 A:PO4335 4.0 27.7 0.8
O4 A:PO4335 4.2 28.5 0.4
ND1 A:HIS24 4.2 19.2 1.0
CG A:HIS24 4.2 20.6 1.0
ND1 A:HIS22 4.2 23.5 1.0
CG A:HIS22 4.2 18.9 1.0
CE1 A:HIS215 4.3 26.4 1.0
NZ A:KCX154 4.4 25.5 1.0
CB A:ALA66 4.4 19.2 1.0
CB A:ASP272 4.5 21.1 1.0
NE2 A:HIS215 4.6 23.9 1.0
CA A:ASP272 5.0 20.4 1.0

Zinc binding site 2 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 2 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


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 the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn334

b:25.3
occ:0.42
OQ2 A:KCX154 1.9 22.3 0.6
ND1 A:HIS187 2.1 21.3 1.0
NE2 A:HIS215 2.2 23.9 1.0
O2 A:PO4335 2.3 27.7 0.8
O3 A:PO4335 2.8 25.3 1.0
CX A:KCX154 3.0 22.9 0.4
CE1 A:HIS187 3.0 23.5 1.0
P A:PO4335 3.1 29.6 0.5
CD2 A:HIS215 3.1 22.7 1.0
CG A:HIS187 3.2 19.5 1.0
CE1 A:HIS215 3.2 26.4 1.0
OQ1 A:KCX154 3.3 25.1 0.9
CB A:HIS187 3.5 21.0 1.0
ND2 A:ASN96 3.6 28.8 1.0
ZN A:ZN333 3.8 26.5 0.6
CE1 A:HIS22 4.0 23.9 1.0
NZ A:KCX154 4.1 25.5 1.0
O1 A:PO4335 4.1 27.9 0.5
O4 A:PO4335 4.2 28.5 0.4
NE2 A:HIS187 4.2 19.7 1.0
NE2 A:HIS22 4.2 20.4 1.0
CD2 A:HIS187 4.3 19.8 1.0
CA A:HIS187 4.3 16.4 1.0
ND1 A:HIS215 4.3 26.3 1.0
CG A:HIS215 4.3 22.4 1.0
CG A:ASN96 4.5 26.5 1.0
CE A:KCX154 4.6 23.0 1.0
OD1 A:ASN96 4.6 30.4 1.0
NZ A:LYS97 4.8 30.8 1.0
OD2 A:ASP272 4.9 26.7 1.0

Zinc binding site 3 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 3 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


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 the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn334

b:28.1
occ:0.66
O3 B:PO4336 2.0 27.6 0.9
NE2 B:HIS24 2.1 23.0 1.0
NE2 B:HIS22 2.2 22.4 1.0
OD1 B:ASP272 2.4 25.4 1.0
OQ1 B:KCX154 2.4 28.0 0.8
CE1 B:HIS24 3.1 22.6 1.0
CD2 B:HIS24 3.1 22.1 1.0
P B:PO4336 3.1 29.3 0.5
CD2 B:HIS22 3.1 21.4 1.0
CE1 B:HIS22 3.2 23.8 1.0
O1 B:PO4336 3.2 27.1 0.6
CG B:ASP272 3.2 24.0 1.0
CX B:KCX154 3.3 24.7 0.5
OD2 B:ASP272 3.5 26.0 1.0
OQ2 B:KCX154 3.6 23.8 0.7
ZN B:ZN335 3.8 24.1 0.4
O2 B:PO4336 3.9 29.9 0.9
ND1 B:HIS24 4.2 21.8 1.0
O4 B:PO4336 4.2 29.0 0.5
CG B:HIS24 4.2 21.6 1.0
CG B:HIS22 4.3 19.1 1.0
ND1 B:HIS22 4.3 23.3 1.0
CE1 B:HIS215 4.3 26.1 1.0
CB B:ALA66 4.5 22.5 1.0
NZ B:KCX154 4.5 24.9 1.0
CB B:ASP272 4.5 20.3 1.0
NE2 B:HIS215 4.6 23.3 1.0
CA B:ASP272 5.0 20.8 1.0

Zinc binding site 4 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 4 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


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 the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn335

b:24.1
occ:0.41
OQ2 B:KCX154 1.9 23.8 0.7
ND1 B:HIS187 2.2 22.4 1.0
NE2 B:HIS215 2.2 23.3 1.0
O2 B:PO4336 2.3 29.9 0.9
O3 B:PO4336 2.8 27.6 0.9
CX B:KCX154 3.0 24.7 0.5
CE1 B:HIS187 3.1 21.3 1.0
P B:PO4336 3.1 29.3 0.5
CD2 B:HIS215 3.2 22.6 1.0
CE1 B:HIS215 3.2 26.1 1.0
CG B:HIS187 3.2 19.3 1.0
OQ1 B:KCX154 3.3 28.0 0.8
CB B:HIS187 3.6 20.4 1.0
OD1 B:ASN96 3.6 31.2 1.0
ZN B:ZN334 3.8 28.1 0.7
CE1 B:HIS22 4.0 23.8 1.0
O1 B:PO4336 4.1 27.1 0.6
NZ B:KCX154 4.1 24.9 1.0
NE2 B:HIS22 4.2 22.4 1.0
O4 B:PO4336 4.2 29.0 0.5
NE2 B:HIS187 4.2 19.2 1.0
CA B:HIS187 4.3 17.0 1.0
ND1 B:HIS215 4.3 26.8 1.0
CD2 B:HIS187 4.3 19.9 1.0
CG B:HIS215 4.3 22.0 1.0
CG B:ASN96 4.5 26.9 1.0
CE B:KCX154 4.6 24.0 1.0
ND2 B:ASN96 4.7 30.0 1.0
OD2 B:ASP272 4.8 26.0 1.0
NZ B:LYS97 4.9 32.0 1.0

Zinc binding site 5 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 5 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn337

b:22.8
occ:0.65
O3 C:PO4339 2.0 23.8 0.9
NE2 C:HIS24 2.0 17.8 1.0
NE2 C:HIS22 2.1 19.3 1.0
OD1 C:ASP272 2.2 20.2 1.0
OQ1 C:KCX154 2.7 20.6 0.8
CD2 C:HIS24 3.0 17.0 1.0
CE1 C:HIS24 3.0 19.0 1.0
CG C:ASP272 3.0 19.7 1.0
CD2 C:HIS22 3.1 18.9 1.0
P C:PO4339 3.1 25.2 0.3
CE1 C:HIS22 3.2 18.6 1.0
O1 C:PO4339 3.3 23.6 0.4
OD2 C:ASP272 3.3 23.2 1.0
CX C:KCX154 3.6 20.1 0.4
ZN C:ZN338 3.8 25.0 0.4
OQ2 C:KCX154 3.8 19.5 0.5
O2 C:PO4339 4.0 25.8 0.6
ND1 C:HIS24 4.1 17.4 1.0
CG C:HIS24 4.2 15.4 1.0
O4 C:PO4339 4.2 29.4 0.5
CG C:HIS22 4.2 15.6 1.0
ND1 C:HIS22 4.3 20.8 1.0
CE1 C:HIS215 4.3 22.9 1.0
CB C:ASP272 4.4 16.8 1.0
NE2 C:HIS215 4.5 22.6 1.0
O C:HOH974 4.6 34.5 1.0
CB C:ALA66 4.7 16.3 1.0
NZ C:KCX154 4.8 20.3 1.0
CA C:ASP272 4.8 17.4 1.0
O C:HOH1550 4.9 41.1 1.0

Zinc binding site 6 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 6 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn338

b:25.0
occ:0.40
OQ2 C:KCX154 2.0 19.5 0.5
NE2 C:HIS215 2.2 22.6 1.0
ND1 C:HIS187 2.2 18.5 1.0
O2 C:PO4339 2.3 25.8 0.6
O3 C:PO4339 2.7 23.8 0.9
CX C:KCX154 3.0 20.1 0.4
P C:PO4339 3.0 25.2 0.3
CE1 C:HIS187 3.1 21.6 1.0
CD2 C:HIS215 3.2 21.2 1.0
CE1 C:HIS215 3.2 22.9 1.0
OQ1 C:KCX154 3.3 20.6 0.8
CG C:HIS187 3.3 16.4 1.0
CB C:HIS187 3.6 17.2 1.0
ZN C:ZN337 3.8 22.8 0.7
OD1 C:ASN96 3.9 37.7 1.0
CE1 C:HIS22 3.9 18.6 1.0
O4 C:PO4339 4.0 29.4 0.5
NE2 C:HIS22 4.1 19.3 1.0
O1 C:PO4339 4.2 23.6 0.4
NZ C:KCX154 4.2 20.3 1.0
NE2 C:HIS187 4.3 17.4 1.0
ND1 C:HIS215 4.3 23.9 1.0
CA C:HIS187 4.3 15.9 1.0
CG C:HIS215 4.3 19.3 1.0
CD2 C:HIS187 4.4 16.7 1.0
ND2 C:ASN96 4.6 31.8 1.0
CE C:KCX154 4.7 20.6 1.0
CG C:ASN96 4.7 29.8 1.0
OD2 C:ASP272 4.8 23.2 1.0
NZ C:LYS97 4.8 28.0 1.0

Zinc binding site 7 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 7 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn334

b:24.7
occ:0.64
O3 D:PO4336 2.0 25.0 0.9
NE2 D:HIS24 2.1 19.1 1.0
NE2 D:HIS22 2.1 19.9 1.0
OD1 D:ASP272 2.2 22.2 1.0
OQ1 D:KCX154 2.6 23.9 0.7
CD2 D:HIS22 3.0 18.5 1.0
CD2 D:HIS24 3.1 19.0 1.0
CE1 D:HIS24 3.1 19.7 1.0
P D:PO4336 3.1 28.6 0.4
CG D:ASP272 3.1 21.4 1.0
CE1 D:HIS22 3.2 20.5 1.0
O1 D:PO4336 3.2 26.2 0.3
OD2 D:ASP272 3.4 25.1 1.0
CX D:KCX154 3.5 23.8 0.3
ZN D:ZN335 3.8 27.0 0.4
OQ2 D:KCX154 3.8 25.0 0.6
O2 D:PO4336 4.0 31.4 0.7
ND1 D:HIS24 4.2 17.1 1.0
O4 D:PO4336 4.2 30.1 0.3
CG D:HIS24 4.2 16.5 1.0
CG D:HIS22 4.2 17.3 1.0
ND1 D:HIS22 4.2 21.5 1.0
CE1 D:HIS215 4.3 24.1 1.0
CB D:ASP272 4.4 18.2 1.0
CB D:ALA66 4.5 18.0 1.0
NE2 D:HIS215 4.5 23.2 1.0
O D:HOH1139 4.5 37.0 1.0
NZ D:KCX154 4.7 24.6 1.0
CA D:ASP272 4.9 17.1 1.0

Zinc binding site 8 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 8 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn335

b:27.0
occ:0.40
OQ2 D:KCX154 2.1 25.0 0.6
ND1 D:HIS187 2.2 20.4 1.0
NE2 D:HIS215 2.2 23.2 1.0
O2 D:PO4336 2.4 31.4 0.7
O3 D:PO4336 2.6 25.0 0.9
CX D:KCX154 3.0 23.8 0.3
P D:PO4336 3.1 28.6 0.4
CE1 D:HIS187 3.1 23.9 1.0
CE1 D:HIS215 3.2 24.1 1.0
CD2 D:HIS215 3.2 21.8 1.0
CG D:HIS187 3.2 18.7 1.0
OQ1 D:KCX154 3.3 23.9 0.7
CB D:HIS187 3.6 20.6 1.0
ZN D:ZN334 3.8 24.7 0.6
CE1 D:HIS22 3.9 20.5 1.0
OD1 D:ASN96 4.0 37.0 1.0
O4 D:PO4336 4.0 30.1 0.3
NE2 D:HIS22 4.1 19.9 1.0
O1 D:PO4336 4.2 26.2 0.3
NZ D:KCX154 4.2 24.6 1.0
NE2 D:HIS187 4.3 20.1 1.0
ND1 D:HIS215 4.3 24.5 1.0
CA D:HIS187 4.3 14.9 1.0
CG D:HIS215 4.3 20.8 1.0
CD2 D:HIS187 4.3 21.9 1.0
ND2 D:ASN96 4.4 31.6 1.0
CE D:KCX154 4.6 25.1 1.0
CG D:ASN96 4.6 36.1 1.0
OD2 D:ASP272 4.8 25.1 1.0
NZ D:LYS97 4.9 33.0 1.0

Zinc binding site 9 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 9 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn335

b:21.6
occ:0.64
O3 E:PO4337 2.0 23.4 0.9
NE2 E:HIS24 2.0 14.7 1.0
NE2 E:HIS22 2.1 17.6 1.0
OD1 E:ASP272 2.3 18.9 1.0
OQ1 E:KCX154 2.6 22.0 0.8
CD2 E:HIS24 3.0 16.3 1.0
CE1 E:HIS24 3.0 16.9 1.0
CG E:ASP272 3.1 20.5 1.0
CD2 E:HIS22 3.1 16.4 1.0
CE1 E:HIS22 3.1 18.6 1.0
P E:PO4337 3.2 25.5 0.3
O1 E:PO4337 3.3 24.3 0.3
OD2 E:ASP272 3.3 21.6 1.0
CX E:KCX154 3.6 19.7 0.5
ZN E:ZN336 3.8 25.6 0.4
OQ2 E:KCX154 3.9 19.8 0.5
O2 E:PO4337 4.1 25.2 0.5
ND1 E:HIS24 4.1 16.0 1.0
CG E:HIS24 4.1 13.8 1.0
O4 E:PO4337 4.2 29.0 0.5
ND1 E:HIS22 4.2 19.6 1.0
CG E:HIS22 4.3 15.4 1.0
CE1 E:HIS215 4.3 21.9 1.0
CB E:ASP272 4.4 17.5 1.0
NE2 E:HIS215 4.5 22.9 1.0
CB E:ALA66 4.6 15.2 1.0
O E:HOH1012 4.7 34.9 1.0
NZ E:KCX154 4.7 20.1 1.0
CA E:ASP272 4.9 16.0 1.0

Zinc binding site 10 out of 12 in 3pnz

Go back to Zinc Binding Sites List in 3pnz
Zinc binding site 10 out of 12 in the Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn336

b:25.6
occ:0.40
OQ2 E:KCX154 2.0 19.8 0.5
NE2 E:HIS215 2.2 22.9 1.0
ND1 E:HIS187 2.3 19.9 1.0
O2 E:PO4337 2.5 25.2 0.5
O3 E:PO4337 2.6 23.4 0.9
CX E:KCX154 3.0 19.7 0.5
P E:PO4337 3.1 25.5 0.3
CE1 E:HIS187 3.1 20.9 1.0
CD2 E:HIS215 3.2 20.1 1.0
CE1 E:HIS215 3.2 21.9 1.0
OQ1 E:KCX154 3.2 22.0 0.8
CG E:HIS187 3.3 18.0 1.0
CB E:HIS187 3.7 16.9 1.0
ZN E:ZN335 3.8 21.6 0.6
ND2 E:ASN96 3.8 31.1 1.0
CE1 E:HIS22 3.9 18.6 1.0
O4 E:PO4337 3.9 29.0 0.5
NE2 E:HIS22 4.1 17.6 1.0
NZ E:KCX154 4.2 20.1 1.0
O1 E:PO4337 4.3 24.3 0.3
NE2 E:HIS187 4.3 19.8 1.0
CA E:HIS187 4.3 15.0 1.0
ND1 E:HIS215 4.3 22.9 1.0
CG E:HIS215 4.4 17.9 1.0
CD2 E:HIS187 4.4 18.7 1.0
CE E:KCX154 4.7 21.0 1.0
CG E:ASN96 4.7 26.5 1.0
OD2 E:ASP272 4.8 21.6 1.0
OD1 E:ASN96 4.8 32.5 1.0
NZ E:LYS97 4.8 29.1 1.0

Reference:

A.A.Fedorov, E.V.Fedorov, D.F.Xiang, F.M.Raushel, S.C.Almo. Crystal Structure of the Lactonase LMO2620 From Listeria Monocytogenes To Be Published.
Page generated: Sat Oct 26 11:37:13 2024

Last articles

Mg in 5X0I
Mg in 5X19
Mg in 5WWD
Mg in 5X06
Mg in 5X0J
Mg in 5X0E
Mg in 5WY5
Mg in 5WW9
Mg in 5WXG
Mg in 5WW8
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy