Calcium in PDB 5c3o: Crystal Structure of the C-Terminal Truncated Neurospora Crassa T7H (NCT7HDELTAC) in Apo Form

The structure of Crystal Structure of the C-Terminal Truncated Neurospora Crassa T7H (NCT7HDELTAC) in Apo Form, PDB code: 5c3o was solved by W.Li, T.Zhang, J.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	119.148, 119.148, 56.631, 90.00, 90.00, 120.00
R / Rfree (%)	19.6 / 22.4

The binding sites of Calcium atom in the Crystal Structure of the C-Terminal Truncated Neurospora Crassa T7H (NCT7HDELTAC) in Apo Form (pdb code 5c3o). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of the C-Terminal Truncated Neurospora Crassa T7H (NCT7HDELTAC) in Apo Form, PDB code: 5c3o:

Calcium binding site 1 out of 1 in the Crystal Structure of the C-Terminal Truncated Neurospora Crassa T7H (NCT7HDELTAC) in Apo Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the C-Terminal Truncated Neurospora Crassa T7H (NCT7HDELTAC) in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca407 b:32.7 occ:1.00 NE2 A:HIS271 2.2 44.2 1.0 OD1 A:ASP216 2.2 47.3 1.0 O A:HOH585 2.3 49.2 1.0 NE2 A:HIS214 2.4 59.3 1.0 O A:HOH563 2.4 46.2 1.0 O A:HOH589 3.0 62.0 1.0 CE1 A:HIS271 3.0 43.4 1.0 CE1 A:HIS214 3.0 58.8 1.0 CG A:ASP216 3.1 43.8 1.0 OD2 A:ASP216 3.2 43.9 1.0 CD2 A:HIS271 3.3 45.0 1.0 CD2 A:HIS214 3.4 59.5 1.0 ND1 A:HIS271 4.2 44.2 1.0 ND1 A:HIS214 4.2 59.8 1.0 CG A:HIS271 4.3 44.5 1.0 CG A:HIS214 4.4 60.2 1.0 CB A:ASP216 4.5 43.6 1.0 N A:ASP216 4.9 44.6 1.0 CA A:ASP216 4.9 43.4 1.0 CE1 A:PHE292 5.0 52.3 1.0

W.Li, T.Zhang, J.Ding. Molecular Basis For the Substrate Specificity and Catalytic Mechanism of Thymine-7-Hydroxylase in Fungi Nucleic Acids Res. V. 43 10026 2015.
ISSN: ESSN 1362-4962
PubMed: 26429971
DOI: 10.1093/NAR/GKV979