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Zinc in PDB 9gl0: Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila

Protein crystallography data

The structure of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila, PDB code: 9gl0 was solved by L.G.Graf, S.Schulze, G.J.Palm, M.Lammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.96 / 2.70
Space group P 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 109.121, 109.121, 400.511, 90, 90, 90
R / Rfree (%) 24 / 31.6

Other elements in 9gl0:

The structure of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila also contains other interesting chemical elements:

Potassium (K) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila (pdb code 9gl0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila, PDB code: 9gl0:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 9gl0

Go back to Zinc Binding Sites List in 9gl0
Zinc binding site 1 out of 4 in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:103.3
occ:0.70
OD1 A:ASP219 2.0 92.6 1.0
OD1 A:ASN221 2.0 99.7 1.0
OD2 A:ASP219 2.3 94.3 1.0
OD2 A:ASP332 2.4 108.5 1.0
CG A:ASP219 2.4 93.4 1.0
CG A:ASN221 3.0 102.0 1.0
CG A:ASP332 3.3 105.8 1.0
OD1 A:ASP332 3.4 100.5 1.0
CB A:ASN221 3.6 102.1 1.0
N A:ASN221 3.8 91.5 1.0
CB A:ASP219 4.0 95.0 1.0
CA A:GLY392 4.0 103.8 1.0
NE2 A:HIS180 4.1 96.2 1.0
ND2 A:ASN221 4.2 104.3 1.0
N A:GLY392 4.2 102.2 1.0
CA A:ASN221 4.3 103.4 1.0
N A:VAL220 4.3 96.5 1.0
CE1 A:HIS180 4.4 96.1 1.0
CG1 A:VAL220 4.6 95.4 1.0
C A:ASP219 4.7 94.1 1.0
CA A:ASP219 4.7 90.6 1.0
CB A:ASP332 4.7 100.5 1.0
NE2 A:HIS181 4.7 100.7 1.0
CE1 A:TYR394 4.8 109.8 1.0
OH A:TYR394 4.8 110.5 1.0
O A:ASN221 4.8 94.8 1.0
C A:VAL220 4.9 89.9 1.0

Zinc binding site 2 out of 4 in 9gl0

Go back to Zinc Binding Sites List in 9gl0
Zinc binding site 2 out of 4 in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:101.8
occ:0.67
OD2 B:ASP332 2.0 110.1 1.0
OD1 B:ASP219 2.3 88.6 1.0
OD1 B:ASN221 2.3 101.3 1.0
OD2 B:ASP219 2.4 88.9 1.0
CG B:ASP219 2.7 93.5 1.0
CG B:ASP332 3.1 105.7 1.0
CG B:ASN221 3.4 104.8 1.0
OD1 B:ASP332 3.7 101.4 1.0
CA B:GLY392 3.8 102.7 1.0
CB B:ASN221 3.9 100.8 1.0
OH B:TYR394 4.0 114.1 1.0
N B:GLY392 4.2 98.5 1.0
CB B:ASP219 4.2 97.2 1.0
N B:ASN221 4.3 102.3 1.0
CB B:ASP332 4.3 107.8 1.0
CE2 B:TYR394 4.3 110.2 1.0
NE2 B:HIS180 4.3 94.6 1.0
ND2 B:ASN221 4.5 104.6 1.0
CZ B:TYR394 4.7 112.8 1.0
CA B:ASN221 4.7 102.9 1.0
N B:VAL220 4.7 94.8 1.0
NE2 B:HIS181 4.8 98.6 1.0
CE1 B:HIS180 4.8 94.5 1.0
C B:GLY392 4.8 109.1 1.0
CG1 B:VAL220 4.9 100.3 1.0
CA B:ASP219 5.0 95.5 1.0

Zinc binding site 3 out of 4 in 9gl0

Go back to Zinc Binding Sites List in 9gl0
Zinc binding site 3 out of 4 in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn501

b:113.5
occ:0.80
O C:HOH601 2.1 111.9 1.0
OD1 C:ASP219 2.3 104.0 1.0
OD1 C:ASN221 2.3 104.5 1.0
O C:HOH604 2.5 118.0 1.0
OD2 C:ASP332 2.5 109.2 1.0
OD2 C:ASP219 2.6 102.3 1.0
CG C:ASP219 2.8 106.0 1.0
O C:HOH602 2.8 99.6 1.0
CG C:ASN221 3.4 108.3 1.0
CG C:ASP332 3.5 109.9 1.0
OH C:TYR394 3.7 110.7 1.0
OD1 C:ASP332 3.8 109.4 1.0
CA C:GLY392 3.9 107.9 1.0
CB C:ASN221 4.0 114.2 1.0
NE2 C:HIS180 4.1 106.8 1.0
CE2 C:TYR394 4.3 115.0 1.0
CB C:ASP219 4.3 106.9 1.0
N C:GLY392 4.3 104.2 1.0
CZ C:TYR394 4.4 117.9 1.0
ND2 C:ASN221 4.5 108.8 1.0
N C:ASN221 4.5 109.7 1.0
CE1 C:HIS180 4.7 111.3 1.0
CB C:ASP332 4.8 112.3 1.0
C C:GLY392 4.8 110.4 1.0
N C:VAL220 4.8 100.4 1.0
CA C:ASN221 4.9 114.0 1.0
N C:GLY393 4.9 110.1 1.0
NE2 C:HIS181 5.0 111.5 1.0

Zinc binding site 4 out of 4 in 9gl0

Go back to Zinc Binding Sites List in 9gl0
Zinc binding site 4 out of 4 in the Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Acetylpolyamine Aminohydrolase (Apah) From Legionella Pneumophila within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn501

b:111.4
occ:0.72
OD2 D:ASP332 2.0 113.4 1.0
OD1 D:ASN221 2.0 102.8 1.0
OD1 D:ASP219 2.4 98.6 1.0
OD2 D:ASP219 2.5 104.4 1.0
CG D:ASP219 2.8 105.3 1.0
O D:HOH603 3.1 99.6 1.0
CG D:ASP332 3.2 111.1 1.0
CG D:ASN221 3.2 105.8 1.0
OD1 D:ASP332 3.7 110.9 1.0
OH D:TYR394 3.8 112.0 1.0
CB D:ASN221 3.9 109.9 1.0
CA D:GLY392 4.0 106.6 1.0
CE2 D:TYR394 4.2 111.9 1.0
NE2 D:HIS180 4.2 100.5 1.0
ND2 D:ASN221 4.3 105.7 1.0
CB D:ASP219 4.3 106.0 1.0
N D:ASN221 4.4 108.8 1.0
CB D:ASP332 4.4 108.2 1.0
N D:GLY392 4.5 104.8 1.0
CZ D:TYR394 4.5 116.3 1.0
CG1 D:VAL220 4.5 103.8 1.0
CE1 D:HIS180 4.7 102.8 1.0
N D:VAL220 4.8 98.3 1.0
CA D:ASN221 4.8 113.0 1.0
NE2 D:HIS181 4.9 110.5 1.0
C D:GLY392 4.9 109.5 1.0

Reference:

L.G.Graf, C.Moreno-Yruela, C.Qin, S.Schulze, G.J.Palm, O.Schmoeker, N.Wang, D.Hocking, L.Jebeli, B.Girbardt, L.Berndt, D.M.Weis, M.Janetzky, D.Zuehlke, S.Sievers, R.A.Strugnell, C.A.Olsen, K.Hofmann, M.Lammers. Distribution and Diversity of Classical Deacylases in Bacteria Nature Communications 2024.
Page generated: Wed Nov 13 13:59:29 2024

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