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Chlorine in PDB 2bje: Acylphosphatase From Sulfolobus Solfataricus. Monclinic P21 Space Group

Enzymatic activity of Acylphosphatase From Sulfolobus Solfataricus. Monclinic P21 Space Group

All present enzymatic activity of Acylphosphatase From Sulfolobus Solfataricus. Monclinic P21 Space Group:
3.6.1.7;

Protein crystallography data

The structure of Acylphosphatase From Sulfolobus Solfataricus. Monclinic P21 Space Group, PDB code: 2bje was solved by C.Rosano, S.Zuccotti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.9
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.980, 56.532, 60.805, 90.00, 103.69, 90.00
R / Rfree (%) 16.2 / 21.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Acylphosphatase From Sulfolobus Solfataricus. Monclinic P21 Space Group (pdb code 2bje). 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 Acylphosphatase From Sulfolobus Solfataricus. Monclinic P21 Space Group, PDB code: 2bje:

Chlorine binding site 1 out of 1 in 2bje

Go back to Chlorine Binding Sites List in 2bje
Chlorine binding site 1 out of 1 in the Acylphosphatase From Sulfolobus Solfataricus. Monclinic P21 Space Group


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Acylphosphatase From Sulfolobus Solfataricus. Monclinic P21 Space Group within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1096

b:71.4
occ:1.00
O A:HOH2010 3.1 40.4 1.0
NH2 A:ARG64 3.4 56.7 1.0
NE A:ARG32 3.6 41.9 1.0
NH2 A:ARG32 3.8 48.4 1.0
ND1 A:HIS29 4.1 44.8 1.0
NE A:ARG64 4.1 56.0 1.0
CZ A:ARG32 4.2 45.8 1.0
CZ A:ARG64 4.2 57.9 1.0
CE1 A:HIS29 4.3 40.0 1.0
CD A:ARG32 4.7 40.5 1.0

Reference:

A.Corazza, C.Rosano, K.Pagano, V.Alverdi, G.Esposito, C.Capanni, F.Bemporad, G.Plakoutsi, M.Stefani, F.Chiti, S.Zuccotti, M.Bolognesi, P.Viglino. Structure, Conformational Stability, and Enzymatic Properties of Acylphosphatase From the Hyperthermophile Sulfolobus Solfataricus. Proteins: Struct., Funct., V. 62 64 2006BIOINF..
ISSN: ISSN 0887-3585
PubMed: 16287076
DOI: 10.1002/PROT.20703
Page generated: Sat Dec 12 09:00:23 2020

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