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Zinc in PDB 1r0c: Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme

Enzymatic activity of Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme

All present enzymatic activity of Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme:
2.1.3.2;

Protein crystallography data

The structure of Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme, PDB code: 1r0c was solved by J.Huang, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.37
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 128.776, 128.776, 198.017, 90.00, 90.00, 120.00
R / Rfree (%) 22.6 / 27.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme (pdb code 1r0c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme, PDB code: 1r0c:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1r0c

Go back to Zinc Binding Sites List in 1r0c
Zinc binding site 1 out of 2 in the Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:30.6
occ:1.00
 SG B:CYS141 2.2 30.9 1.0
SG B:CYS138 2.2 30.0 1.0
SG B:CYS109 2.3 31.8 1.0
SG B:CYS114 2.4 32.5 1.0
CB B:CYS138 2.9 35.9 1.0
CB B:CYS114 3.1 31.9 1.0
CB B:CYS141 3.2 29.7 1.0
CB B:CYS109 3.4 33.6 1.0
N B:CYS141 3.5 29.6 1.0
CA B:CYS141 3.9 29.6 1.0
CA B:CYS114 4.4 32.0 1.0
CA B:CYS138 4.4 35.3 1.0
CB B:TYR140 4.6 28.1 1.0
C B:TYR140 4.7 30.5 1.0
CB B:ASN111 4.7 29.9 1.0
ND2 B:ASN111 4.7 31.2 1.0
OG B:SER116 4.7 34.1 1.0
O B:HOH1050 4.8 37.1 1.0
C B:CYS141 4.8 31.5 1.0
CA B:CYS109 4.8 33.6 1.0
N B:GLU142 4.8 33.8 1.0
CA B:TYR140 5.0 30.1 1.0

Zinc binding site 2 out of 2 in 1r0c

Go back to Zinc Binding Sites List in 1r0c
Zinc binding site 2 out of 2 in the Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn1002

b:27.4
occ:1.00
 SG H:CYS141 2.2 24.7 1.0
SG H:CYS109 2.2 36.6 1.0
SG H:CYS114 2.3 30.9 1.0
SG H:CYS138 2.3 24.9 1.0
CB H:CYS138 3.0 34.8 1.0
CB H:CYS114 3.2 29.3 1.0
CB H:CYS141 3.2 25.6 1.0
CB H:CYS109 3.4 35.1 1.0
N H:CYS141 3.7 27.5 1.0
CA H:CYS141 4.0 26.2 1.0
CA H:CYS114 4.4 30.1 1.0
CB H:ASN111 4.5 32.5 1.0
CA H:CYS138 4.5 35.0 1.0
ND2 H:ASN111 4.6 32.4 1.0
CB H:TYR140 4.7 28.3 1.0
OG H:SER116 4.7 34.5 1.0
CA H:CYS109 4.8 35.1 1.0
C H:TYR140 4.8 29.0 1.0
C H:CYS141 4.9 28.3 1.0
N H:GLU142 5.0 29.0 1.0

Reference:

J.Huang, W.N.Lipscomb. Products in the T-State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-Carbamyl-L-Aspartate Ligated Enzyme Biochemistry V. 43 6422 2004.
ISSN: ISSN 0006-2960
PubMed: 15157076
DOI: 10.1021/BI0302144
Page generated: Wed Oct 16 18:18:26 2024

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