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Zinc in PDB 1shq: Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3

Enzymatic activity of Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3

All present enzymatic activity of Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3:
3.1.3.1;

Protein crystallography data

The structure of Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3, PDB code: 1shq was solved by M.M.E.De Backer, S.Mcsweeney, P.F.Lindley, E.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.53 / 2.00
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 171.007, 171.007, 84.098, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 23.8

Other elements in 1shq:

The structure of Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3 also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3 (pdb code 1shq). 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 Shrimp Alkaline Phosphatase with Magnesium in M3, PDB code: 1shq:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1shq

Go back to Zinc Binding Sites List in 1shq
Zinc binding site 1 out of 4 in the Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3


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 Shrimp Alkaline Phosphatase with Magnesium in M3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn484

b:33.4
occ:1.00
O2 A:SO4486 1.3 26.1 0.5
NE2 A:HIS319 1.9 21.2 1.0
OD2 A:ASP315 2.0 25.1 1.0
NE2 A:HIS432 2.1 23.3 1.0
O4 A:SO4486 2.2 34.2 0.5
S A:SO4486 2.2 34.7 0.5
CG A:ASP315 2.8 25.8 1.0
OD1 A:ASP315 2.8 22.1 1.0
CE1 A:HIS319 2.8 23.3 1.0
CD2 A:HIS319 3.0 24.1 1.0
CD2 A:HIS432 3.0 25.1 1.0
CE1 A:HIS432 3.2 23.5 1.0
O1 A:SO4486 3.2 37.7 0.5
O3 A:SO4486 3.3 32.5 0.5
ND1 A:HIS319 4.0 26.5 1.0
CG A:HIS319 4.1 23.5 1.0
CG A:HIS432 4.2 22.0 1.0
ND1 A:HIS432 4.2 23.3 1.0
CB A:ASP315 4.2 23.3 1.0
CE1 A:HIS357 4.4 23.8 1.0
CE1 A:HIS359 4.4 24.4 1.0
OG A:SER86 4.4 27.5 1.0
NE2 A:HIS357 4.4 22.8 1.0
OD1 A:ASP37 4.7 25.8 1.0
ZN A:ZN485 4.7 32.4 0.3
O A:ASP315 5.0 22.1 1.0

Zinc binding site 2 out of 4 in 1shq

Go back to Zinc Binding Sites List in 1shq
Zinc binding site 2 out of 4 in the Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3


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 Shrimp Alkaline Phosphatase with Magnesium in M3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn485

b:32.4
occ:0.32
OG A:SER86 1.8 27.5 1.0
OD2 A:ASP356 1.9 23.1 1.0
OD1 A:ASP37 2.1 25.8 1.0
NE2 A:HIS357 2.1 22.8 1.0
OD2 A:ASP37 2.6 26.3 1.0
CG A:ASP37 2.6 27.5 1.0
CD2 A:HIS357 2.8 20.1 1.0
CG A:ASP356 2.8 21.7 1.0
CB A:SER86 3.0 23.2 1.0
OD1 A:ASP356 3.1 17.9 1.0
CE1 A:HIS357 3.2 23.8 1.0
CA A:SER86 3.5 22.8 1.0
O2 A:SO4486 3.7 26.1 0.5
O A:HOH495 4.0 19.1 1.0
CB A:ASP37 4.0 21.9 1.0
CG A:HIS357 4.0 21.1 1.0
N A:SER86 4.0 22.8 1.0
CE1 A:HIS432 4.1 23.5 1.0
CB A:ASP356 4.2 21.5 1.0
ND1 A:HIS357 4.2 22.1 1.0
OD2 A:ASP315 4.2 25.1 1.0
CG A:ASP315 4.3 25.8 1.0
O A:HOH537 4.3 38.0 1.0
N A:GLY38 4.3 20.1 1.0
CA A:ASP37 4.4 22.2 1.0
MG A:MG479 4.4 30.5 1.0
NE2 A:HIS432 4.4 23.3 1.0
OD1 A:ASP315 4.5 22.1 1.0
S A:SO4486 4.5 34.7 0.5
C A:ASP37 4.5 20.5 1.0
O3 A:SO4486 4.7 32.5 0.5
O A:HOH538 4.7 35.6 1.0
ZN A:ZN484 4.7 33.4 1.0
C A:SER86 4.8 23.0 1.0
C A:ASP85 4.8 22.2 1.0
CB A:ASP315 4.8 23.3 1.0
O1 A:SO4486 4.8 37.7 0.5
OG1 A:THR151 4.9 20.4 1.0
ND1 A:HIS432 4.9 23.3 1.0
OG A:SER89 5.0 23.3 1.0

Zinc binding site 3 out of 4 in 1shq

Go back to Zinc Binding Sites List in 1shq
Zinc binding site 3 out of 4 in the Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3


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 Shrimp Alkaline Phosphatase with Magnesium in M3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn480

b:32.5
occ:1.00
O2 B:SO4487 1.8 29.3 0.5
NE2 B:HIS319 2.0 19.9 1.0
NE2 B:HIS432 2.1 22.4 1.0
OD2 B:ASP315 2.1 22.9 1.0
O1 B:SO4487 2.2 35.6 0.5
S B:SO4487 2.4 36.5 0.5
CG B:ASP315 2.8 26.1 1.0
OD1 B:ASP315 2.8 22.5 1.0
CE1 B:HIS319 2.9 23.9 1.0
CD2 B:HIS319 3.0 24.2 1.0
CD2 B:HIS432 3.0 25.1 1.0
CE1 B:HIS432 3.1 24.2 1.0
O4 B:SO4487 3.3 33.9 0.5
O3 B:SO4487 3.5 38.8 0.5
ND1 B:HIS319 4.1 25.7 1.0
CG B:HIS319 4.1 24.2 1.0
ND1 B:HIS432 4.2 21.0 1.0
CG B:HIS432 4.2 22.2 1.0
CE1 B:HIS357 4.3 24.7 1.0
CB B:ASP315 4.3 23.1 1.0
NE2 B:HIS357 4.3 21.6 1.0
OG B:SER86 4.4 25.4 1.0
NE2 B:HIS359 4.5 26.2 1.0
ZN B:ZN481 4.5 27.1 0.3
OD1 B:ASP37 4.6 26.6 1.0
CE1 B:HIS359 4.9 24.5 1.0

Zinc binding site 4 out of 4 in 1shq

Go back to Zinc Binding Sites List in 1shq
Zinc binding site 4 out of 4 in the Crystal Structure of Shrimp Alkaline Phosphatase with Magnesium in M3


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 Shrimp Alkaline Phosphatase with Magnesium in M3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn481

b:27.1
occ:0.32
OG B:SER86 1.9 25.4 1.0
OD1 B:ASP37 1.9 26.6 1.0
NE2 B:HIS357 2.0 21.6 1.0
OD2 B:ASP356 2.1 22.5 1.0
CG B:ASP37 2.6 26.9 1.0
OD2 B:ASP37 2.7 25.6 1.0
CD2 B:HIS357 2.7 18.9 1.0
CG B:ASP356 2.9 22.5 1.0
CE1 B:HIS357 3.0 24.7 1.0
OD1 B:ASP356 3.0 19.4 1.0
CB B:SER86 3.1 23.4 1.0
CA B:SER86 3.5 22.4 1.0
O2 B:SO4487 3.6 29.3 0.5
CG B:HIS357 3.9 21.3 1.0
ND1 B:HIS357 4.0 22.1 1.0
CE1 B:HIS432 4.0 24.2 1.0
CB B:ASP37 4.0 22.4 1.0
N B:SER86 4.1 22.5 1.0
OD2 B:ASP315 4.1 22.9 1.0
O B:HOH497 4.2 18.0 1.0
CG B:ASP315 4.2 26.1 1.0
CB B:ASP356 4.2 20.3 1.0
N B:GLY38 4.2 19.5 1.0
OD1 B:ASP315 4.3 22.5 1.0
NE2 B:HIS432 4.4 22.4 1.0
CA B:ASP37 4.4 21.7 1.0
ZN B:ZN480 4.5 32.5 1.0
O B:HOH538 4.5 33.0 1.0
C B:ASP37 4.5 20.7 1.0
MG B:MG482 4.6 32.6 1.0
CB B:ASP315 4.8 23.1 1.0
C B:ASP85 4.8 22.4 1.0
ND1 B:HIS432 4.8 21.0 1.0
C B:SER86 4.9 22.2 1.0
OG B:SER89 4.9 21.2 1.0
S B:SO4487 5.0 36.5 0.5
CA B:GLY38 5.0 19.2 1.0

Reference:

M.M.De Backer, S.Mcsweeney, P.F.Lindley, E.Hough. Ligand-Binding and Metal-Exchange Crystallographic Studies on Shrimp Alkaline Phosphatase. Acta Crystallogr.,Sect.D V. 60 1555 2004.
ISSN: ISSN 0907-4449
PubMed: 15333925
DOI: 10.1107/S0907444904015628
Page generated: Wed Dec 16 03:03:39 2020

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