Zinc in PDB 8aq0: Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C

Enzymatic activity of Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C

All present enzymatic activity of Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C:
3.5.1.87;

Protein crystallography data

The structure of Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C, PDB code: 8aq0 was solved by H.J.Rozeboom, C.Mayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 99.23 / 2.30
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 132.569, 42.047, 137.211, 90, 94.78, 90
R / Rfree (%) 17.3 / 23.8

Other elements in 8aq0:

The structure of Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C (pdb code 8aq0). 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 L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C, PDB code: 8aq0:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 8aq0

Go back to Zinc Binding Sites List in 8aq0
Zinc binding site 1 out of 4 in the Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C


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 L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:47.6
occ:0.44
 FE A:FE502 0.6 35.4 0.2
OD1 A:ASP98 2.0 40.9 1.0
O A:HOH636 2.1 32.8 1.0
N1 A:NV6505 2.2 60.7 1.0
NE2 A:HIS194 2.3 46.4 1.0
NE2 A:HIS87 2.4 41.9 1.0
O1 A:NV6505 2.6 53.4 1.0
C1 A:NV6505 2.7 66.8 1.0
CG A:ASP98 3.2 40.4 1.0
CE1 A:HIS194 3.2 47.6 1.0
CE1 A:HIS87 3.3 39.3 1.0
CD2 A:HIS194 3.3 47.4 1.0
CD2 A:HIS87 3.4 40.0 1.0
FE A:FE504 3.5 39.2 0.2
ZN A:ZN503 3.5 45.3 0.4
OE1 A:GLU132 3.7 47.0 1.0
OD2 A:ASP98 3.7 41.9 1.0
N2 A:NV6505 3.9 70.7 1.0
CD A:GLU132 4.0 43.4 1.0
N A:GLY99 4.0 42.4 1.0
ND1 A:HIS362 4.1 46.5 1.0
OE2 A:GLU132 4.1 44.7 1.0
OE2 A:GLU133 4.3 41.6 1.0
ND1 A:HIS194 4.4 43.0 1.0
OE1 A:GLN197 4.4 37.4 1.0
CG A:HIS194 4.4 44.3 1.0
ND1 A:HIS87 4.5 37.7 1.0
CE1 A:HIS362 4.5 47.7 1.0
CB A:ASP98 4.5 39.4 1.0
CA A:GLY99 4.5 40.6 1.0
C A:ASP98 4.5 38.9 1.0
CG A:HIS87 4.5 38.5 1.0
NE2 A:GLN197 4.6 35.5 1.0
O A:HOH604 4.7 38.4 1.0
CD A:GLU133 4.7 37.7 1.0
CA A:ASP98 4.7 37.3 1.0
OE1 A:GLU133 4.8 43.7 1.0
CD A:GLN197 4.8 38.1 1.0
CG A:GLU132 4.9 45.8 1.0
O A:GLY361 4.9 43.3 1.0

Zinc binding site 2 out of 4 in 8aq0

Go back to Zinc Binding Sites List in 8aq0
Zinc binding site 2 out of 4 in the Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C


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 L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn503

b:45.3
occ:0.44
 FE A:FE504 0.1 39.2 0.2
OD2 A:ASP98 2.0 41.9 1.0
O1 A:NV6505 2.0 53.4 1.0
OE2 A:GLU133 2.1 41.6 1.0
OE1 A:GLU133 2.1 43.7 1.0
NE2 A:HIS386 2.2 45.4 1.0
CD A:GLU133 2.4 37.7 1.0
C1 A:NV6505 2.6 66.8 1.0
CG A:ASP98 2.8 40.4 1.0
N1 A:NV6505 3.0 60.7 1.0
OD1 A:ASP98 3.1 40.9 1.0
CD2 A:HIS386 3.2 43.3 1.0
CE1 A:HIS386 3.2 41.5 1.0
ZN A:ZN501 3.5 47.6 0.4
N2 A:NV6505 3.7 70.7 1.0
NE2 A:GLN197 3.8 35.5 1.0
FE A:FE502 3.8 35.4 0.2
CG A:GLU133 3.9 38.6 1.0
OE1 A:GLU132 4.1 47.0 1.0
O A:HOH634 4.2 43.5 1.0
CB A:ASP98 4.2 39.4 1.0
ND1 A:HIS386 4.3 40.7 1.0
CG A:HIS386 4.3 40.5 1.0
C2 A:NV6505 4.4 72.5 1.0
CE1 A:HIS87 4.4 39.3 1.0
NE2 A:HIS87 4.5 41.9 1.0
CD2 B:HIS230 4.5 46.3 1.0
NE2 B:HIS230 4.6 45.8 1.0
CG A:GLN91 4.8 35.8 1.0
NE2 A:GLN91 4.8 30.9 1.0
CD A:GLN197 4.8 38.1 1.0
CB A:GLU133 4.9 36.4 1.0
O4 A:NV6505 5.0 68.8 1.0
OE1 A:GLN197 5.0 37.4 1.0

Zinc binding site 3 out of 4 in 8aq0

Go back to Zinc Binding Sites List in 8aq0
Zinc binding site 3 out of 4 in the Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C


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 L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:41.7
occ:0.44
 FE B:FE502 0.1 37.5 0.2
OD1 B:ASP98 2.1 40.9 1.0
N1 B:NV6505 2.1 55.9 1.0
NE2 B:HIS194 2.1 44.8 1.0
O B:HOH631 2.2 31.6 1.0
NE2 B:HIS87 2.2 45.5 1.0
CE1 B:HIS194 3.1 47.3 1.0
CD2 B:HIS194 3.1 44.1 1.0
CG B:ASP98 3.2 40.5 1.0
CD2 B:HIS87 3.2 43.2 1.0
CE1 B:HIS87 3.2 48.0 1.0
C1 B:NV6505 3.4 64.6 1.0
FE B:FE504 3.7 37.1 0.2
ZN B:ZN503 3.7 44.1 0.4
OE1 B:GLU132 3.8 46.4 1.0
OD2 B:ASP98 3.8 43.1 1.0
N B:GLY99 3.9 40.4 1.0
O1 B:NV6505 3.9 55.2 1.0
ND1 B:HIS362 4.1 35.8 1.0
CD B:GLU132 4.1 46.3 1.0
CA B:GLY99 4.2 37.8 1.0
ND1 B:HIS194 4.2 45.4 1.0
CG B:HIS194 4.3 43.7 1.0
OE2 B:GLU132 4.3 47.7 1.0
OE2 B:GLU133 4.4 45.0 1.0
N2 B:NV6505 4.4 68.6 1.0
ND1 B:HIS87 4.4 46.0 1.0
C B:ASP98 4.4 41.3 1.0
CG B:HIS87 4.4 45.3 1.0
O B:HOH604 4.4 33.6 1.0
CB B:ASP98 4.5 40.3 1.0
CE1 B:HIS362 4.5 37.8 1.0
OE1 B:GLN197 4.6 48.6 1.0
CA B:ASP98 4.7 38.6 1.0
NE2 B:GLN197 4.8 45.7 1.0
CD B:GLU133 4.9 43.0 1.0
CG B:GLU132 4.9 46.2 1.0
CD B:GLN197 5.0 48.7 1.0

Zinc binding site 4 out of 4 in 8aq0

Go back to Zinc Binding Sites List in 8aq0
Zinc binding site 4 out of 4 in the Crystal Structure of L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C


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 L-N-Carbamoylase From Sinorhizobium Meliloti Mutant L217G/F329C within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn503

b:44.1
occ:0.44
 FE B:FE504 0.1 37.1 0.2
O1 B:NV6505 2.0 55.2 1.0
OD2 B:ASP98 2.0 43.1 1.0
OE1 B:GLU133 2.1 45.9 1.0
OE2 B:GLU133 2.1 45.0 1.0
NE2 B:HIS386 2.2 43.1 1.0
CD B:GLU133 2.4 43.0 1.0
C1 B:NV6505 2.7 64.6 1.0
N1 B:NV6505 2.9 55.9 1.0
CG B:ASP98 2.9 40.5 1.0
CE1 B:HIS386 3.2 42.6 1.0
CD2 B:HIS386 3.2 42.6 1.0
OD1 B:ASP98 3.2 40.9 1.0
FE B:FE502 3.6 37.5 0.2
ZN B:ZN501 3.7 41.7 0.4
CG B:GLU133 3.9 41.2 1.0
N2 B:NV6505 3.9 68.6 1.0
NE2 B:GLN197 3.9 45.7 1.0
O B:HOH622 4.1 33.8 1.0
OE1 B:GLU132 4.1 46.4 1.0
CB B:ASP98 4.3 40.3 1.0
ND1 B:HIS386 4.3 39.0 1.0
CG B:HIS386 4.4 40.7 1.0
CE1 B:HIS87 4.4 48.0 1.0
CD2 A:HIS230 4.5 51.8 1.0
NE2 A:HIS230 4.5 53.0 1.0
NE2 B:HIS87 4.6 45.5 1.0
C2 B:NV6505 4.6 81.6 1.0
CG B:GLN91 4.7 38.2 1.0
NE2 B:GLN91 4.8 37.3 1.0
CB B:GLU133 4.8 39.7 1.0
O B:HOH639 4.9 42.5 1.0
CD B:GLN197 4.9 48.7 1.0

Reference:

R.Rubini, S.C.Jansen, H.Beekhuis, H.J.Rozeboom, C.Mayer. Selecting Better Biocatalysts By Complementing Recoded Bacteria. Angew.Chem.Int.Ed.Engl. 13942 2022.
ISSN: ESSN 1521-3773
PubMed: 36342942
DOI: 10.1002/ANIE.202213942
Page generated: Wed Oct 30 17:57:54 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy