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Zinc in PDB 3pm6: Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr

Enzymatic activity of Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr

All present enzymatic activity of Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr:
4.1.2.13;

Protein crystallography data

The structure of Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr, PDB code: 3pm6 was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.910, 77.770, 68.320, 90.00, 93.71, 90.00
R / Rfree (%) 19.8 / 23.7

Other elements in 3pm6:

The structure of Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr also contains other interesting chemical elements:

Iodine (I) 33 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr (pdb code 3pm6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr, PDB code: 3pm6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3pm6

Go back to Zinc Binding Sites List in 3pm6
Zinc binding site 1 out of 2 in the Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr


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 A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn319

b:20.8
occ:1.00
ND1 A:HIS223 2.1 9.2 1.0
NE2 A:HIS87 2.1 13.2 1.0
NE2 A:HIS192 2.2 13.8 1.0
CE1 A:HIS223 3.0 11.3 1.0
CE1 A:HIS87 3.0 11.0 1.0
CD2 A:HIS192 3.1 12.9 1.0
CD2 A:HIS87 3.2 10.5 1.0
CG A:HIS223 3.2 12.1 1.0
CE1 A:HIS192 3.2 12.9 1.0
CB A:HIS223 3.6 13.6 1.0
NE2 A:HIS223 4.1 12.4 1.0
ND1 A:HIS87 4.1 11.6 1.0
OD2 A:ASP86 4.2 13.4 1.0
CG A:HIS192 4.2 15.7 1.0
CG A:HIS87 4.3 12.8 1.0
ND1 A:HIS192 4.3 14.9 1.0
CD2 A:HIS223 4.3 10.1 1.0
ND2 A:ASN245 4.3 10.4 1.0
OD1 A:ASP86 4.4 13.3 1.0
CA A:HIS223 4.4 14.7 1.0
N A:GLY224 4.7 13.7 1.0
CG A:ASP86 4.7 13.6 1.0

Zinc binding site 2 out of 2 in 3pm6

Go back to Zinc Binding Sites List in 3pm6
Zinc binding site 2 out of 2 in the Crystal Structure of A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr


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 A Putative Fructose-1,6-Biphosphate Aldolase From Coccidioides Immitis Solved By Combined Sad Mr within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn320

b:47.8
occ:1.00
NE2 B:HIS87 2.1 30.8 1.0
ND1 B:HIS223 2.3 32.1 1.0
O B:HOH400 2.5 22.3 1.0
O B:HOH403 2.9 23.1 1.0
O B:HOH402 2.9 18.4 1.0
CE1 B:HIS87 3.0 30.1 1.0
CD2 B:HIS87 3.1 27.7 1.0
CG B:HIS223 3.3 33.1 1.0
CE1 B:HIS223 3.3 31.4 1.0
CB B:HIS223 3.5 34.1 1.0
O B:HOH401 3.8 28.0 1.0
ND1 B:HIS87 4.2 29.8 1.0
CG B:HIS87 4.2 26.4 1.0
OD2 B:ASP86 4.3 24.7 1.0
ND2 B:ASN245 4.3 23.4 1.0
NE2 B:HIS223 4.4 32.8 1.0
CD2 B:HIS223 4.4 33.1 1.0
CA B:HIS223 4.5 34.7 1.0
O B:HOH410 4.6 24.0 1.0
OD1 B:ASP86 4.7 22.9 1.0
N B:GLY224 4.8 37.3 1.0
CG B:ASP86 5.0 24.3 1.0

Reference:

J.Abendroth, A.S.Gardberg, J.I.Robinson, J.S.Christensen, B.L.Staker, P.J.Myler, L.J.Stewart, T.E.Edwards. Sad Phasing Using Iodide Ions in A High-Throughput Structural Genomics Environment. J Struct Funct Genomics V. 12 83 2011.
PubMed: 21359836
DOI: 10.1007/S10969-011-9101-7
Page generated: Wed Dec 16 04:43:19 2020

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