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Zinc in PDB 2ada: Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations

Enzymatic activity of Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations

All present enzymatic activity of Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations:
3.5.4.4;

Protein crystallography data

The structure of Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations, PDB code: 2ada was solved by D.K.Wilson, F.A.Quiocho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 102.360, 94.110, 72.930, 90.00, 127.19, 90.00
R / Rfree (%) 19.5 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations (pdb code 2ada). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations, PDB code: 2ada:

Zinc binding site 1 out of 1 in 2ada

Go back to Zinc Binding Sites List in 2ada
Zinc binding site 1 out of 1 in the Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:12.4
occ:1.00
 NE2 A:HIS17 2.2 2.5 1.0
NE2 A:HIS214 2.2 2.0 1.0
O6 A:HPR353 2.3 10.4 1.0
NE2 A:HIS15 2.3 12.1 1.0
OD2 A:ASP295 2.4 4.7 1.0
CE1 A:HIS17 3.0 2.0 1.0
CD2 A:HIS214 3.1 5.5 1.0
CD2 A:HIS17 3.2 5.4 1.0
CE1 A:HIS214 3.2 4.9 1.0
CE1 A:HIS15 3.2 11.2 1.0
CD2 A:HIS15 3.3 12.3 1.0
C6 A:HPR353 3.3 7.2 1.0
C5 A:HPR353 3.4 3.4 1.0
CG A:ASP295 3.4 9.1 1.0
OD1 A:ASP295 3.7 10.3 1.0
N7 A:HPR353 3.7 3.7 1.0
NE2 A:HIS238 3.8 4.7 1.0
N1 A:HPR353 3.9 8.5 1.0
C4 A:HPR353 4.0 2.6 1.0
ND1 A:HIS17 4.1 2.1 1.0
CG A:HIS17 4.3 2.0 1.0
CG A:HIS214 4.3 3.7 1.0
ND1 A:HIS214 4.3 7.0 1.0
ND1 A:HIS15 4.3 12.4 1.0
CG A:HIS15 4.4 11.5 1.0
C2 A:HPR353 4.4 5.8 1.0
C8 A:HPR353 4.4 4.6 1.0
N3 A:HPR353 4.5 6.3 1.0
CE1 A:HIS238 4.6 2.1 1.0
N9 A:HPR353 4.6 3.2 1.0
CD2 A:HIS238 4.7 6.0 1.0
OD2 A:ASP296 4.7 8.0 1.0
CB A:ASP295 4.8 6.4 1.0
NH2 A:ARG101 4.8 12.4 1.0
CD A:ARG101 4.8 4.2 1.0

Reference:

D.K.Wilson, F.B.Rudolph, F.A.Quiocho. Atomic Structure of Adenosine Deaminase Complexed with A Transition-State Analog: Understanding Catalysis and Immunodeficiency Mutations. Science V. 252 1278 1991.
ISSN: ISSN 0036-8075
PubMed: 1925539
Page generated: Wed Oct 16 21:36:10 2024

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