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Zinc in PDB 2aq2: Crystal Structure of T-Cell Receptor V Beta Domain Variant Complexed with Superantigen SEC3 Mutant

Protein crystallography data

The structure of Crystal Structure of T-Cell Receptor V Beta Domain Variant Complexed with Superantigen SEC3 Mutant, PDB code: 2aq2 was solved by S.Cho, C.P.Swaminathan, J.Yang, M.C.Kerzic, R.Guan, M.C.Kieke, D.M.Kranz, R.A.Mariuzza, E.J.Sundberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.80
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 96.537, 96.537, 92.182, 90.00, 90.00, 120.00
R / Rfree (%) 18.5 / 21.3

Other elements in 2aq2:

The structure of Crystal Structure of T-Cell Receptor V Beta Domain Variant Complexed with Superantigen SEC3 Mutant also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of T-Cell Receptor V Beta Domain Variant Complexed with Superantigen SEC3 Mutant (pdb code 2aq2). 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 Crystal Structure of T-Cell Receptor V Beta Domain Variant Complexed with Superantigen SEC3 Mutant, PDB code: 2aq2:

Zinc binding site 1 out of 1 in 2aq2

Go back to Zinc Binding Sites List in 2aq2
Zinc binding site 1 out of 1 in the Crystal Structure of T-Cell Receptor V Beta Domain Variant Complexed with Superantigen SEC3 Mutant


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 T-Cell Receptor V Beta Domain Variant Complexed with Superantigen SEC3 Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:54.1
occ:1.00
NE2 B:HIS120 1.9 36.9 1.0
ND1 B:HIS116 2.1 32.9 1.0
OD2 B:ASP83 2.2 23.5 1.0
CE1 B:HIS116 2.7 34.7 1.0
OD1 B:ASP83 2.7 22.2 1.0
CG B:ASP83 2.7 20.6 1.0
CE1 B:HIS120 2.8 38.3 1.0
CD2 B:HIS120 2.9 36.8 1.0
CG B:HIS116 3.1 31.2 1.0
NE2 B:HIS116 3.7 33.6 1.0
CB B:HIS116 3.8 26.8 1.0
CA B:HIS116 3.9 26.6 1.0
ND1 B:HIS120 3.9 38.3 1.0
CG B:HIS120 4.0 37.5 1.0
CD2 B:HIS116 4.0 33.6 1.0
O B:HIS116 4.0 26.8 1.0
CG2 B:THR36 4.0 30.2 1.0
O B:HOH1014 4.2 22.9 1.0
CB B:ASP83 4.2 17.8 1.0
C B:HIS116 4.3 27.5 1.0
N B:LYS37 5.0 25.4 1.0

Reference:

S.Cho, C.P.Swaminathan, J.Yang, M.C.Kerzic, R.Guan, M.C.Kieke, D.M.Kranz, R.A.Mariuzza, E.J.Sundberg. Structural Basis of Affinity Maturation and Intramolecular Cooperativity in A Protein-Protein Interaction. Structure V. 13 1775 2005.
ISSN: ISSN 0969-2126
PubMed: 16338399
DOI: 10.1016/J.STR.2005.08.015
Page generated: Wed Dec 16 03:17:45 2020

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