Zinc in PDB 6sj0: Amidohydrolase, Ahs

Protein crystallography data

The structure of Amidohydrolase, Ahs, PDB code: 6sj0 was solved by J.H.Naismith, H.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.81 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 81.790, 82.750, 141.560, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 20.9

Zinc Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 22;

Binding sites:

The binding sites of Zinc atom in the Amidohydrolase, Ahs (pdb code 6sj0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 22 binding sites of Zinc where determined in the Amidohydrolase, Ahs, PDB code: 6sj0:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 22 in 6sj0

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Zinc binding site 1 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn504

b:22.5
occ:1.00
NE2 A:HIS75 2.0 22.6 1.0
NE2 A:HIS77 2.0 21.4 1.0
NE2 A:HIS253 2.0 22.2 1.0
O A:HOH627 2.2 29.9 1.0
OD1 A:ASP345 2.6 34.2 1.0
CD2 A:HIS253 2.9 23.5 1.0
CE1 A:HIS75 3.0 34.2 1.0
CD2 A:HIS75 3.0 25.4 1.0
CE1 A:HIS77 3.0 27.6 1.0
CD2 A:HIS77 3.0 22.0 1.0
CE1 A:HIS253 3.1 24.9 1.0
CG A:ASP345 3.5 33.6 1.0
OD2 A:ASP345 3.9 35.0 1.0
ND1 A:HIS75 4.1 31.1 1.0
NE2 A:HIS290 4.1 27.3 1.0
CG A:HIS253 4.1 21.9 1.0
CG A:HIS75 4.1 22.3 1.0
ND1 A:HIS77 4.1 24.8 1.0
ND1 A:HIS253 4.2 27.6 1.0
CG A:HIS77 4.2 21.5 1.0
CB A:ASP345 4.6 25.8 1.0
CA A:ASP345 4.7 22.6 1.0
CE1 A:HIS290 4.8 25.0 1.0
CD2 A:HIS290 4.9 29.7 1.0

Zinc binding site 2 out of 22 in 6sj0

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Zinc binding site 2 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn505

b:0.2
occ:1.00
O A:HOH763 3.1 46.0 1.0
OE2 A:GLU41 4.9 63.8 1.0

Zinc binding site 3 out of 22 in 6sj0

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Zinc binding site 3 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn506

b:56.6
occ:1.00
O A:HOH777 2.4 49.1 1.0
O A:HOH776 2.5 47.4 1.0
CD2 A:HIS246 2.6 43.3 1.0
CG A:HIS246 3.3 45.2 1.0
CB A:HIS246 3.4 37.5 1.0
NE2 A:HIS246 3.7 54.5 1.0
CA A:HIS246 3.9 33.0 1.0
O A:HIS246 4.3 34.9 1.0
CD2 A:LEU208 4.3 39.9 1.0
ND1 A:HIS246 4.5 52.1 1.0
C A:HIS246 4.6 32.1 1.0
CE1 A:HIS246 4.8 47.4 1.0
CG A:LEU208 5.0 38.0 1.0

Zinc binding site 4 out of 22 in 6sj0

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Zinc binding site 4 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn507

b:64.2
occ:1.00
ND1 A:HIS110 2.2 45.8 1.0
O A:HOH773 2.6 58.9 1.0
O A:HOH768 2.6 50.9 1.0
O A:HOH774 2.7 54.0 1.0
CE1 A:HIS110 3.0 43.0 1.0
O A:HOH750 3.0 56.8 1.0
CG A:HIS110 3.2 37.2 1.0
CB A:HIS110 3.6 34.1 1.0
CB A:PRO186 4.1 43.8 1.0
NE2 A:HIS110 4.2 42.6 1.0
CD2 A:HIS110 4.3 46.2 1.0
OD1 A:ASP108 4.4 33.0 1.0
CG A:PRO186 4.8 39.2 1.0
O A:HOH702 5.0 43.1 1.0
CA A:HIS110 5.0 30.5 1.0

Zinc binding site 5 out of 22 in 6sj0

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Zinc binding site 5 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn508

b:83.4
occ:1.00
OD1 A:ASP395 2.4 33.0 1.0
OD2 A:ASP395 3.0 34.9 1.0
CG A:ASP395 3.0 31.7 1.0
CB A:ASP395 4.5 27.7 1.0
CG A:LYS390 4.5 32.1 1.0
O A:LYS390 4.6 25.3 1.0
CA A:ARG393 4.8 28.3 1.0
CA A:LYS390 4.8 23.8 1.0
N A:ASP395 4.9 24.4 1.0

Zinc binding site 6 out of 22 in 6sj0

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Zinc binding site 6 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn509

b:0.3
occ:1.00
CE1 A:HIS21 2.9 41.2 1.0
O A:HOH684 3.0 39.8 1.0
NE2 A:HIS21 3.3 41.9 1.0
ND1 A:HIS21 4.1 33.6 1.0
CD2 A:HIS21 4.6 37.9 1.0
CA A:GLY37 4.6 30.6 1.0
CD A:PRO38 4.7 37.4 1.0
O A:VAL36 4.7 28.5 1.0
OE1 A:GLU41 4.8 51.6 1.0
OG A:SER19 5.0 39.5 1.0
CG A:HIS21 5.0 33.5 1.0

Zinc binding site 7 out of 22 in 6sj0

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Zinc binding site 7 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn510

b:90.2
occ:1.00
OE2 A:GLU278 2.6 59.9 1.0
CD A:GLU278 3.6 63.8 1.0
OE1 A:GLU278 4.0 63.6 1.0
CB A:GLU270 4.9 34.0 1.0
CG A:GLU278 4.9 53.6 1.0
CG A:GLU270 4.9 36.9 1.0
OE1 A:GLU270 5.0 49.4 1.0

Zinc binding site 8 out of 22 in 6sj0

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Zinc binding site 8 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn511

b:85.0
occ:1.00
OD1 A:ASP296 2.6 55.2 1.0
CG A:ASP296 3.5 50.8 1.0
OD2 A:ASP296 3.7 54.4 1.0
NE2 A:GLN299 4.3 27.6 1.0
OE1 A:GLN299 4.7 36.6 1.0
CD A:GLN299 4.9 33.6 1.0
CB A:ASP296 5.0 44.4 1.0

Zinc binding site 9 out of 22 in 6sj0

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Zinc binding site 9 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn512

b:0.8
occ:1.00
O A:HOH741 3.7 36.2 1.0
O A:HOH661 4.6 27.5 1.0
OG1 A:THR10 4.7 28.3 1.0
O A:ASN422 4.7 24.1 1.0
OG1 A:THR414 4.8 26.9 1.0
O A:HOH704 4.9 34.9 1.0
O A:HOH609 4.9 30.7 1.0

Zinc binding site 10 out of 22 in 6sj0

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Zinc binding site 10 out of 22 in the Amidohydrolase, Ahs


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Amidohydrolase, Ahs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn513

b:55.4
occ:1.00
OE2 A:GLU205 4.3 50.1 1.0
OE1 A:GLU205 4.3 46.9 1.0
CD A:GLU205 4.8 49.8 1.0
O A:HOH766 4.9 40.5 1.0

Reference:

H.Song, C.Rao, Z.Deng, Y.Yi, J.H.Naismith. The Biosynthetic Pathway of the Benzoxazole in Nataxazole Proceeds Via An Unstable Ester and Has Synthetic Utility. Angew.Chem.Int.Ed.Engl. 2020.
ISSN: ESSN 1521-3773
PubMed: 31903677
DOI: 10.1002/ANIE.201915685
Page generated: Wed Dec 16 12:48:37 2020

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