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Zinc in PDB 1d09: Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala)

Enzymatic activity of Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala)

All present enzymatic activity of Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala):
2.1.3.2;

Protein crystallography data

The structure of Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala), PDB code: 1d09 was solved by L.Jin, B.Stec, W.N.Lipscomb, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.10
Space group P 3 2 1
Cell size a, b, c (Å), α, β, γ (°) 122.240, 122.240, 156.360, 90.00, 90.00, 120.00
R / Rfree (%) 20.3 / 23.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala) (pdb code 1d09). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala), PDB code: 1d09:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1d09

Go back to Zinc Binding Sites List in 1d09
Zinc binding site 1 out of 2 in the Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1313

b:26.3
occ:1.00
SG B:CYS141 2.2 27.6 1.0
SG B:CYS109 2.3 27.2 1.0
SG B:CYS114 2.3 26.7 1.0
SG B:CYS138 2.3 24.8 1.0
CB B:CYS138 2.9 22.2 1.0
CB B:CYS114 3.2 11.7 1.0
CB B:CYS141 3.3 21.5 1.0
CB B:CYS109 3.3 24.4 1.0
N B:CYS141 3.6 17.3 1.0
CA B:CYS141 4.0 16.2 1.0
OG B:SER116 4.2 15.9 1.0
CB B:ASN111 4.3 26.6 1.0
CA B:CYS138 4.4 27.9 1.0
CA B:CYS114 4.5 13.1 1.0
O B:HOH1411 4.6 33.0 1.0
ND2 B:ASN111 4.7 26.9 1.0
CA B:CYS109 4.7 26.2 1.0
C B:TYR140 4.7 13.3 1.0
CB B:TYR140 4.8 6.4 1.0
C B:CYS141 4.9 18.8 1.0
CG B:ASN111 4.9 24.5 1.0
CZ B:PHE145 5.0 41.1 1.0

Zinc binding site 2 out of 2 in 1d09

Go back to Zinc Binding Sites List in 1d09
Zinc binding site 2 out of 2 in the Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aspartate Transcarbamoylase Complexed with N-Phosphonacetyl-L- Aspartate (Pala) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1314

b:23.9
occ:1.00
SG D:CYS138 2.2 21.4 1.0
SG D:CYS114 2.3 20.3 1.0
SG D:CYS141 2.3 20.3 1.0
SG D:CYS109 2.3 17.5 1.0
CB D:CYS138 3.1 24.9 1.0
CB D:CYS114 3.1 22.5 1.0
CB D:CYS109 3.2 19.0 1.0
CB D:CYS141 3.5 17.4 1.0
N D:CYS141 3.7 14.2 1.0
CA D:CYS141 4.2 12.1 1.0
CA D:CYS114 4.4 22.9 1.0
OG D:SER116 4.4 15.0 1.0
CA D:CYS138 4.5 22.5 1.0
CB D:ASN111 4.6 18.4 1.0
ND2 D:ASN111 4.7 22.8 1.0
CA D:CYS109 4.7 20.9 1.0
CB D:TYR140 4.7 14.4 1.0
O D:HOH1340 4.8 29.6 1.0
C D:TYR140 4.8 18.3 1.0
O D:ASN111 5.0 14.5 1.0

Reference:

L.Jin, B.Stec, W.N.Lipscomb, E.R.Kantrowitz. Insights Into the Mechanisms of Catalysis and Heterotropic Regulation of Escherichia Coli Aspartate Transcarbamoylase Based Upon A Structure of the Enzyme Complexed with the Bisubstrate Analogue N-Phosphonacetyl-L-Aspartate at 2.1 A. Proteins V. 37 729 1999.
ISSN: ISSN 0887-3585
PubMed: 10651286
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<729::AID-PROT21>3.3.CO;2-6
Page generated: Mon Jan 25 16:08:12 2021

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