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Zinc in PDB 5w0r: Crystal Structure of Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid

Enzymatic activity of Crystal Structure of Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid

All present enzymatic activity of Crystal Structure of Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid:
3.5.4.38;

Protein crystallography data

The structure of Crystal Structure of Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid, PDB code: 5w0r was solved by Q.Qiao, L.Wang, H.Wu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.81 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.960, 179.070, 188.080, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 23.9

Other elements in 5w0r:

The structure of Crystal Structure of Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid also contains other interesting chemical elements:

Arsenic (As) 2 atoms
Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid (pdb code 5w0r). 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 Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid, PDB code: 5w0r:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5w0r

Go back to Zinc Binding Sites List in 5w0r
Zinc binding site 1 out of 2 in the Crystal Structure of Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid


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 Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2001

b:36.3
occ:1.00
O1 B:CAC2002 2.0 30.1 1.0
ND1 B:HIS1056 2.2 43.1 1.0
SG B:CYS1090 2.3 42.5 1.0
SG B:CYS1087 2.4 40.1 1.0
CG B:HIS1056 3.1 41.5 1.0
CE1 B:HIS1056 3.1 45.2 1.0
CB B:CYS1090 3.2 41.9 1.0
CB B:HIS1056 3.4 39.1 1.0
AS B:CAC2002 3.4 43.2 1.0
CB B:CYS1087 3.5 45.8 1.0
N B:CYS1087 3.9 42.2 1.0
O B:HOH2127 3.9 24.1 1.0
C1 B:CAC2002 4.0 29.8 1.0
NE2 B:HIS1056 4.1 45.4 1.0
CD2 B:HIS1056 4.1 43.0 1.0
O2 B:CAC2002 4.2 39.4 1.0
N B:CYS1090 4.2 45.5 1.0
CA B:CYS1090 4.3 43.2 1.0
CA B:CYS1087 4.3 44.9 1.0
C B:CYS1087 4.9 46.2 1.0
CA B:HIS1056 4.9 38.8 1.0
C2 B:CAC2002 4.9 26.6 1.0
O B:CYS1087 5.0 44.8 1.0

Zinc binding site 2 out of 2 in 5w0r

Go back to Zinc Binding Sites List in 5w0r
Zinc binding site 2 out of 2 in the Crystal Structure of Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid


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 Mbp Fused Activation-Induced Cytidine Deaminase (Aid) in Complex with Cacodylic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2001

b:42.1
occ:1.00
O1 A:CAC2002 2.0 58.3 1.0
ND1 A:HIS1056 2.0 46.6 1.0
SG A:CYS1090 2.4 37.4 1.0
SG A:CYS1087 2.4 47.7 1.0
CG A:HIS1056 3.0 45.7 1.0
CE1 A:HIS1056 3.0 48.9 1.0
AS A:CAC2002 3.3 49.2 1.0
CB A:HIS1056 3.3 44.3 1.0
CB A:CYS1090 3.4 38.9 1.0
CB A:CYS1087 3.4 43.7 1.0
C1 A:CAC2002 3.7 33.7 1.0
O A:HOH2131 3.9 31.6 1.0
N A:CYS1087 3.9 39.5 1.0
O2 A:CAC2002 4.0 53.1 1.0
NE2 A:HIS1056 4.1 49.2 1.0
CD2 A:HIS1056 4.1 47.0 1.0
CA A:CYS1087 4.2 42.8 1.0
N A:CYS1090 4.2 41.9 1.0
CA A:CYS1090 4.4 40.4 1.0
O A:CYS1087 4.6 41.6 1.0
C A:CYS1087 4.7 43.6 1.0
CA A:HIS1056 4.9 44.8 1.0
C2 A:CAC2002 4.9 33.7 1.0

Reference:

Q.Qiao, L.Wang, F.L.Meng, J.K.Hwang, F.W.Alt, H.Wu. Aid Recognizes Structured Dna For Class Switch Recombination. Mol. Cell V. 67 361 2017.
ISSN: ISSN 1097-4164
PubMed: 28757211
DOI: 10.1016/J.MOLCEL.2017.06.034
Page generated: Mon Oct 28 13:37:22 2024

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