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Zinc in PDB 1r0b: 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: 1r0b 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 / 2.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 120.694, 155.400, 194.957, 90.00, 90.00, 90.00
R / Rfree (%) 24 / 30

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 1r0b). 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: 1r0b:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 1r0b

Go back to Zinc Binding Sites List in 1r0b
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:Zn1001

b:57.7
occ:1.00
SG G:CYS141 2.4 52.2 1.0
SG G:CYS114 2.4 41.9 1.0
SG G:CYS109 2.4 52.6 1.0
SG G:CYS138 2.4 58.8 1.0
CB G:CYS109 3.0 54.5 1.0
CB G:CYS114 3.0 48.7 1.0
CB G:CYS141 3.0 52.6 1.0
O G:CYS141 3.2 56.7 1.0
CB G:CYS138 3.2 57.3 1.0
N G:CYS141 3.6 51.6 1.0
CA G:CYS141 3.6 53.0 1.0
C G:CYS141 3.8 55.6 1.0
OG G:SER116 4.2 60.2 1.0
CA G:CYS114 4.4 51.9 1.0
CA G:CYS109 4.4 54.3 1.0
CA G:CYS138 4.7 57.2 1.0
CB G:ASN111 4.8 53.4 1.0
C G:TYR140 4.8 50.1 1.0

Zinc binding site 2 out of 6 in 1r0b

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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:Zn1002

b:56.9
occ:1.00
CB H:CYS114 2.3 63.9 1.0
SG H:CYS141 2.5 63.1 1.0
SG H:CYS138 2.5 62.4 1.0
SG H:CYS114 2.5 62.0 1.0
SG H:CYS109 2.5 67.4 1.0
CB H:CYS109 2.9 64.9 1.0
CB H:CYS141 3.2 56.8 1.0
CB H:CYS138 3.5 60.5 1.0
CA H:CYS114 3.8 66.3 1.0
N H:CYS141 3.9 52.1 1.0
OG H:SER116 4.1 64.3 1.0
CB H:SER116 4.2 67.1 1.0
CA H:CYS141 4.2 53.7 1.0
N H:CYS114 4.4 67.0 1.0
CA H:CYS109 4.4 65.7 1.0
OD1 H:ASN111 4.6 57.1 1.0
CB H:ASN111 4.7 62.2 1.0
CA H:CYS138 4.7 58.1 1.0
C H:CYS114 4.8 67.6 1.0
CB H:TYR140 4.9 46.4 1.0
O H:ASN111 4.9 69.5 1.0

Zinc binding site 3 out of 6 in 1r0b

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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:Zn1003

b:67.8
occ:1.00
CB I:CYS141 2.2 66.6 1.0
SG I:CYS114 2.4 68.7 1.0
SG I:CYS141 2.4 71.0 1.0
SG I:CYS109 2.5 79.0 1.0
CB I:CYS109 2.5 70.2 1.0
SG I:CYS138 2.5 64.7 1.0
CB I:CYS114 3.0 65.4 1.0
CB I:CYS138 3.2 60.9 1.0
CA I:CYS141 3.4 65.9 1.0
N I:CYS141 3.4 65.4 1.0
CA I:CYS109 4.0 67.8 1.0
OG I:SER116 4.1 61.1 1.0
CA I:CYS114 4.3 62.8 1.0
CB I:ASN111 4.4 64.1 1.0
C I:CYS141 4.4 65.3 1.0
C I:TYR140 4.6 63.0 1.0
CA I:CYS138 4.7 60.5 1.0
N I:GLU142 4.8 65.2 1.0
N I:CYS109 4.8 66.7 1.0
CB I:TYR140 4.8 63.3 1.0
C I:CYS109 4.8 65.3 1.0
OD1 I:ASN111 4.9 64.7 1.0

Zinc binding site 4 out of 6 in 1r0b

Go back to Zinc Binding Sites List in 1r0b
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:Zn1004

b:52.0
occ:1.00
CB J:CYS114 2.1 69.7 1.0
SG J:CYS138 2.3 64.2 1.0
CB J:CYS138 2.4 58.5 1.0
SG J:CYS109 2.5 80.2 1.0
SG J:CYS141 2.5 51.1 1.0
SG J:CYS114 2.5 75.5 1.0
CB J:CYS109 2.9 73.2 1.0
CB J:CYS141 3.3 56.5 1.0
CA J:CYS114 3.5 67.7 1.0
N J:CYS141 3.8 57.7 1.0
CA J:CYS138 3.9 60.8 1.0
CA J:CYS141 4.1 58.8 1.0
N J:CYS114 4.4 64.5 1.0
CA J:CYS109 4.4 68.4 1.0
C J:CYS114 4.4 67.7 1.0
O J:CYS141 4.5 62.1 1.0
CB J:SER116 4.6 64.4 1.0
CB J:ASN111 4.6 58.9 1.0
C J:CYS138 4.7 60.5 1.0
O J:CYS114 4.7 67.3 1.0
N J:CYS138 4.8 63.1 1.0
CB J:TYR140 4.8 49.0 1.0
C J:CYS141 4.8 61.1 1.0
O J:CYS138 4.9 60.3 1.0
C J:TYR140 4.9 54.1 1.0

Zinc binding site 5 out of 6 in 1r0b

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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:Zn1005

b:64.5
occ:1.00
SG K:CYS141 2.4 55.4 1.0
SG K:CYS114 2.4 59.2 1.0
SG K:CYS109 2.4 53.8 1.0
SG K:CYS138 2.5 56.9 1.0
CB K:CYS141 2.8 55.5 1.0
CB K:CYS109 2.8 56.8 1.0
CB K:CYS114 3.2 57.9 1.0
CB K:CYS138 3.4 56.8 1.0
N K:CYS141 3.5 54.0 1.0
CA K:CYS141 3.8 55.5 1.0
OG K:SER116 3.9 46.2 1.0
CA K:CYS109 4.3 58.2 1.0
CB K:SER116 4.5 48.5 1.0
CA K:CYS114 4.6 56.6 1.0
CA K:CYS138 4.7 55.5 1.0
C K:TYR140 4.7 51.8 1.0
C K:CYS141 4.8 56.6 1.0
CB K:TYR140 4.8 48.7 1.0
C K:CYS109 4.9 60.5 1.0
N K:GLU142 5.0 61.2 1.0
CB K:ASN111 5.0 60.5 1.0

Zinc binding site 6 out of 6 in 1r0b

Go back to Zinc Binding Sites List in 1r0b
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:Zn1006

b:63.4
occ:1.00
CB L:CYS141 2.2 69.5 1.0
SG L:CYS109 2.4 83.3 1.0
SG L:CYS114 2.4 69.8 1.0
SG L:CYS138 2.4 56.6 1.0
SG L:CYS141 2.4 74.4 1.0
CB L:CYS138 2.6 62.1 1.0
CB L:CYS114 3.3 71.9 1.0
CB L:CYS109 3.3 78.2 1.0
CA L:CYS141 3.5 69.6 1.0
N L:CYS141 3.5 68.0 1.0
CA L:CYS138 4.1 64.3 1.0
OG L:SER116 4.3 75.0 1.0
C L:CYS141 4.3 70.7 1.0
CB L:ASN111 4.4 63.0 1.0
CA L:CYS114 4.6 71.3 1.0
N L:GLU142 4.7 72.0 1.0
ND2 L:ASN111 4.7 62.4 1.0
C L:CYS138 4.7 64.5 1.0
CA L:CYS109 4.7 76.3 1.0
C L:TYR140 4.8 66.8 1.0
N L:CYS138 4.9 66.8 1.0
CE2 L:PHE145 4.9 92.6 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: Mon Jan 25 16:12:31 2021

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