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Chlorine in PDB 7spg: Crystal Structure of Sperm Whale Myoglobin Variant SMB13(Pcaaf) in Space Group P212121

Protein crystallography data

The structure of Crystal Structure of Sperm Whale Myoglobin Variant SMB13(Pcaaf) in Space Group P212121, PDB code: 7spg was solved by J.P.Bacik, R.Fasan, N.Ando, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.73 / 1.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.492, 56.512, 65.994, 90, 90, 90
R / Rfree (%) 16 / 18.2

Other elements in 7spg:

The structure of Crystal Structure of Sperm Whale Myoglobin Variant SMB13(Pcaaf) in Space Group P212121 also contains other interesting chemical elements:

Iron (Fe) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Sperm Whale Myoglobin Variant SMB13(Pcaaf) in Space Group P212121 (pdb code 7spg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Sperm Whale Myoglobin Variant SMB13(Pcaaf) in Space Group P212121, PDB code: 7spg:

Chlorine binding site 1 out of 1 in 7spg

Go back to Chlorine Binding Sites List in 7spg
Chlorine binding site 1 out of 1 in the Crystal Structure of Sperm Whale Myoglobin Variant SMB13(Pcaaf) in Space Group P212121


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Sperm Whale Myoglobin Variant SMB13(Pcaaf) in Space Group P212121 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl204

b:21.3
occ:1.00
O A:HOH388 3.1 27.2 1.0
N A:ALA127 3.3 19.8 1.0
N A:CYS126 3.3 20.0 1.0
C A:GLY124 3.4 19.8 1.0
CA A:GLY124 3.5 21.0 1.0
CB A:CYS126 3.5 20.4 1.0
N A:GLY124 3.7 20.3 1.0
O A:GLY124 3.8 21.2 1.0
CA A:CYS126 3.8 20.4 1.0
N A:ALA125 3.8 20.5 1.0
CB A:ALA127 4.0 20.9 1.0
C A:CYS126 4.0 19.3 1.0
SG A:CYS126 4.3 21.3 1.0
CA A:ALA127 4.3 19.4 1.0
C A:ALA125 4.3 20.0 1.0
CA A:ALA125 4.7 19.5 1.0
CD2 A:LEU9 4.8 26.6 1.0
C A:PHE123 5.0 22.2 1.0
C2 A:A3U5 5.0 22.5 1.0

Reference:

J.A.Iannuzzelli, J.P.Bacik, E.J.Moore, Z.Shen, E.M.Irving, D.A.Vargas, S.D.Khare, N.Ando, R.Fasan. Tuning Enzyme Thermostability Via Computationally Guided Covalent Stapling and Structural Basis of Enhanced Stabilization. Biochemistry V. 61 1041 2022.
ISSN: ISSN 0006-2960
PubMed: 35612958
DOI: 10.1021/ACS.BIOCHEM.2C00033
Page generated: Sun Jul 13 07:09:49 2025

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