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Zinc in PDB 1q95: Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate

Enzymatic activity of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate

All present enzymatic activity of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate:
2.1.3.2;

Protein crystallography data

The structure of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate, PDB code: 1q95 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) 8.00 / 2.46
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 125.510, 153.490, 185.710, 90.00, 90.00, 90.00
R / Rfree (%) 23 / 27

Zinc Binding Sites:

The binding sites of Zinc atom in the Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate (pdb code 1q95). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate, PDB code: 1q95:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 1q95

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Zinc binding site 1 out of 6 in the Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn2002

b:49.0
occ:1.00
 SG G:CYS114 2.3 41.1 1.0
SG G:CYS141 2.3 42.0 1.0
SG G:CYS109 2.3 49.1 1.0
SG G:CYS138 2.3 48.8 1.0
CB G:CYS114 2.9 43.2 1.0
CB G:CYS109 3.0 48.6 1.0
CB G:CYS138 3.2 46.3 1.0
N G:CYS141 3.5 40.8 1.0
CB G:CYS141 3.6 39.0 1.0
OG G:SER116 4.1 50.1 1.0
CA G:CYS141 4.2 38.6 1.0
CA G:CYS114 4.2 45.6 1.0
CB G:TYR140 4.4 38.4 1.0
CA G:CYS109 4.4 49.8 1.0
C G:TYR140 4.5 40.8 1.0
CA G:CYS138 4.6 44.0 1.0
O G:HOH2003 4.8 49.9 1.0
CA G:TYR140 4.8 40.6 1.0
CB G:SER116 4.8 51.4 1.0
ND2 G:ASN111 4.8 52.8 1.0
O G:HOH2016 4.9 55.5 1.0
N G:TYR140 4.9 40.1 1.0
CB G:ASN111 4.9 51.0 1.0

Zinc binding site 2 out of 6 in 1q95

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Zinc binding site 2 out of 6 in the Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn2001

b:50.2
occ:1.00
 SG H:CYS141 2.2 45.0 1.0
SG H:CYS138 2.2 37.3 1.0
SG H:CYS114 2.3 38.8 1.0
SG H:CYS109 2.3 46.6 1.0
CB H:CYS114 2.9 44.2 1.0
CB H:CYS138 3.0 39.6 1.0
CB H:CYS109 3.3 45.6 1.0
CB H:CYS141 3.3 44.0 1.0
N H:CYS141 3.6 43.5 1.0
CA H:CYS141 4.0 43.5 1.0
CA H:CYS114 4.2 46.6 1.0
CB H:ASN111 4.2 48.1 1.0
OG H:SER116 4.4 53.7 1.0
CA H:CYS138 4.5 41.4 1.0
CB H:TYR140 4.5 48.3 1.0
CA H:CYS109 4.6 47.8 1.0
C H:TYR140 4.7 45.3 1.0
OD1 H:ASN111 4.7 45.5 1.0
N H:TYR140 4.9 46.9 1.0
C H:CYS141 4.9 44.2 1.0
CA H:TYR140 4.9 46.5 1.0
CG H:ASN111 4.9 46.4 1.0

Zinc binding site 3 out of 6 in 1q95

Go back to Zinc Binding Sites List in 1q95
Zinc binding site 3 out of 6 in the Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn2003

b:51.4
occ:1.00
 SG I:CYS114 2.2 54.5 1.0
SG I:CYS141 2.3 49.6 1.0
SG I:CYS109 2.3 58.1 1.0
SG I:CYS138 2.3 42.3 1.0
CB I:CYS138 2.9 44.2 1.0
CB I:CYS114 3.1 53.5 1.0
CB I:CYS109 3.3 58.5 1.0
CB I:CYS141 3.5 52.7 1.0
N I:CYS141 3.7 52.2 1.0
CA I:CYS141 4.2 53.7 1.0
ND2 I:ASN111 4.4 67.8 1.0
CA I:CYS138 4.4 46.8 1.0
CA I:CYS114 4.5 54.2 1.0
OG I:SER116 4.5 57.6 1.0
CB I:TYR140 4.6 47.2 1.0
CA I:CYS109 4.7 58.7 1.0
CB I:ASN111 4.7 64.6 1.0
C I:TYR140 4.8 51.0 1.0
N I:TYR140 4.9 47.1 1.0
C I:CYS141 4.9 56.6 1.0
C I:CYS138 5.0 45.2 1.0

Zinc binding site 4 out of 6 in 1q95

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Zinc binding site 4 out of 6 in the Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn2004

b:52.0
occ:1.00
 SG J:CYS138 2.2 48.0 1.0
SG J:CYS141 2.3 47.1 1.0
SG J:CYS114 2.3 56.2 1.0
SG J:CYS109 2.3 61.6 1.0
CB J:CYS109 2.9 59.8 1.0
CB J:CYS114 3.0 58.6 1.0
CB J:CYS138 3.1 46.8 1.0
CB J:CYS141 3.1 48.1 1.0
N J:CYS141 3.5 47.4 1.0
CA J:CYS141 3.9 48.4 1.0
OG J:SER116 4.2 67.3 1.0
CA J:CYS109 4.3 62.3 1.0
CA J:CYS114 4.5 60.5 1.0
ND2 J:ASN111 4.5 62.6 1.0
CA J:CYS138 4.6 47.8 1.0
CB J:TYR140 4.6 47.3 1.0
C J:TYR140 4.7 49.9 1.0
CB J:ASN111 4.8 61.4 1.0
C J:CYS141 4.8 49.1 1.0
CB J:SER116 4.9 66.7 1.0
N J:GLU142 4.9 47.8 1.0
CA J:TYR140 5.0 48.2 1.0

Zinc binding site 5 out of 6 in 1q95

Go back to Zinc Binding Sites List in 1q95
Zinc binding site 5 out of 6 in the Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Zn2005

b:53.6
occ:1.00
 SG K:CYS114 2.2 56.4 1.0
SG K:CYS141 2.3 54.0 1.0
SG K:CYS138 2.3 49.6 1.0
SG K:CYS109 2.3 65.1 1.0
CB K:CYS114 2.9 56.9 1.0
CB K:CYS141 3.1 51.3 1.0
CB K:CYS109 3.2 63.6 1.0
CB K:CYS138 3.2 53.4 1.0
N K:CYS141 3.6 53.3 1.0
CA K:CYS141 3.9 52.5 1.0
CB K:ASN111 4.2 63.5 1.0
CA K:CYS114 4.2 57.0 1.0
OG K:SER116 4.4 64.5 1.0
ND2 K:ASN111 4.5 63.1 1.0
CA K:CYS109 4.7 64.1 1.0
CG K:ASN111 4.7 62.7 1.0
CA K:CYS138 4.7 56.0 1.0
C K:CYS141 4.8 52.6 1.0
C K:TYR140 4.8 52.9 1.0
CB K:TYR140 4.8 52.8 1.0
CB K:SER116 4.9 64.9 1.0
N K:GLU142 5.0 55.0 1.0

Zinc binding site 6 out of 6 in 1q95

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Zinc binding site 6 out of 6 in the Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R State Bound to Pala, or to Product Analogues Phosphate and Citrate within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Zn2006

b:53.9
occ:1.00
 SG L:CYS109 2.2 59.0 1.0
SG L:CYS138 2.3 51.8 1.0
SG L:CYS141 2.3 53.6 1.0
SG L:CYS114 2.3 44.7 1.0
CB L:CYS138 2.7 63.5 1.0
CB L:CYS109 3.1 61.9 1.0
CB L:CYS114 3.3 46.2 1.0
CB L:CYS141 3.5 56.0 1.0
N L:CYS141 3.9 56.6 1.0
ND2 L:ASN111 4.1 63.1 1.0
OG L:SER116 4.2 51.6 1.0
CA L:CYS138 4.2 66.1 1.0
CA L:CYS141 4.3 56.8 1.0
CB L:ASN111 4.4 60.8 1.0
CA L:CYS114 4.5 48.4 1.0
CA L:CYS109 4.6 63.1 1.0
CG L:ASN111 4.8 60.6 1.0
O L:ASN111 4.9 61.1 1.0
C L:CYS138 5.0 65.1 1.0
CB L:TYR140 5.0 56.0 1.0

Reference:

J.Huang, W.N.Lipscomb. Aspartate Transcarbamylase (Atcase) of Escherichia Coli: A New Crystalline R-State Bound to Pala, or to Product Analogues Citrate and Phosphate Biochemistry V. 43 6415 2004.
ISSN: ISSN 0006-2960
PubMed: 15157075
DOI: 10.1021/BI030213B
Page generated: Wed Oct 16 18:05:56 2024

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