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Zinc in PDB 3a3o: Crystal Structure of Complex Between Sa-Subtilisin and Tk-Propeptide with Deletion of the Five C-Terminal Residues

Protein crystallography data

The structure of Crystal Structure of Complex Between Sa-Subtilisin and Tk-Propeptide with Deletion of the Five C-Terminal Residues, PDB code: 3a3o was solved by S.Tanaka, H.Matsumura, Y.Koga, K.Takano, S.Kanaya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.25 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.478, 68.494, 73.874, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 20.8

Other elements in 3a3o:

The structure of Crystal Structure of Complex Between Sa-Subtilisin and Tk-Propeptide with Deletion of the Five C-Terminal Residues also contains other interesting chemical elements:

Calcium (Ca) 7 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Complex Between Sa-Subtilisin and Tk-Propeptide with Deletion of the Five C-Terminal Residues (pdb code 3a3o). 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 Complex Between Sa-Subtilisin and Tk-Propeptide with Deletion of the Five C-Terminal Residues, PDB code: 3a3o:

Zinc binding site 1 out of 1 in 3a3o

Go back to Zinc Binding Sites List in 3a3o
Zinc binding site 1 out of 1 in the Crystal Structure of Complex Between Sa-Subtilisin and Tk-Propeptide with Deletion of the Five C-Terminal Residues


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 Complex Between Sa-Subtilisin and Tk-Propeptide with Deletion of the Five C-Terminal Residues within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn65

b:33.9
occ:1.00
OD2 B:ASP42 2.1 24.3 1.0
NE2 B:HIS28 2.1 25.0 1.0
O B:HOH105 2.3 37.4 1.0
O B:HOH67 2.3 41.5 1.0
CE1 B:HIS28 2.9 25.5 1.0
CG B:ASP42 3.0 21.0 1.0
CD2 B:HIS28 3.2 24.8 1.0
CB B:ASP42 3.3 19.6 1.0
ND1 B:HIS28 4.1 24.1 1.0
NH2 B:ARG7 4.2 20.9 1.0
OD1 B:ASP42 4.2 18.4 1.0
CG B:HIS28 4.3 22.9 1.0
CG2 B:VAL30 4.6 16.4 1.0
CA B:ASP42 4.8 19.9 1.0

Reference:

S.Tanaka, H.Matsumura, Y.Koga, K.Takano, S.Kanaya. Identification of the Interactions Critical For Propeptide-Catalyzed Folding of Tk-Subtilisin J.Mol.Biol. V. 394 306 2009.
ISSN: ISSN 0022-2836
PubMed: 19766655
DOI: 10.1016/J.JMB.2009.09.028
Page generated: Thu Oct 24 11:02:12 2024

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