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Chlorine in PDB 1mu0: Crystal Structure of the Tricorn Interacting Factor F1 Complex with Pck

Enzymatic activity of Crystal Structure of the Tricorn Interacting Factor F1 Complex with Pck

All present enzymatic activity of Crystal Structure of the Tricorn Interacting Factor F1 Complex with Pck:
3.4.11.5;

Protein crystallography data

The structure of Crystal Structure of the Tricorn Interacting Factor F1 Complex with Pck, PDB code: 1mu0 was solved by P.Goettig, M.Groll, J.-S.Kim, R.Huber, H.Brandstetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.579, 61.721, 80.435, 90.00, 90.00, 90.00
R / Rfree (%) 31.4 / 36.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Tricorn Interacting Factor F1 Complex with Pck (pdb code 1mu0). 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 the Tricorn Interacting Factor F1 Complex with Pck, PDB code: 1mu0:

Chlorine binding site 1 out of 1 in 1mu0

Go back to Chlorine Binding Sites List in 1mu0
Chlorine binding site 1 out of 1 in the Crystal Structure of the Tricorn Interacting Factor F1 Complex with Pck


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 the Tricorn Interacting Factor F1 Complex with Pck within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl300

b:25.4
occ:1.00
CL A:PHK300 0.0 25.4 1.0
C1 A:PHK300 1.8 24.2 1.0
C A:PHK300 2.8 21.4 1.0
CB A:SER105 3.1 16.8 1.0
O A:PHK300 3.2 23.6 1.0
OG A:SER105 3.2 24.9 1.0
NE2 A:HIS271 3.4 26.7 1.0
OH A:TYR44 3.6 15.9 1.0
SD A:MET40 3.8 23.1 1.0
CD2 A:HIS271 3.8 24.7 1.0
N A:GLY37 3.8 9.2 1.0
CA A:GLY36 3.8 12.3 1.0
CA A:PHK300 4.1 25.4 1.0
CZ A:TYR44 4.1 12.0 1.0
C A:GLY36 4.3 11.3 1.0
CE2 A:TYR44 4.4 17.5 1.0
N A:GLY36 4.4 12.9 1.0
CD2 A:LEU272 4.4 21.6 1.0
N A:PHK300 4.4 21.6 1.0
CE1 A:HIS271 4.6 24.3 1.0
CA A:SER105 4.6 15.2 1.0
CE A:MET40 4.7 20.6 1.0
O A:SER104 4.8 13.1 1.0
CA A:GLY37 4.9 8.3 1.0
CE1 A:TYR44 4.9 16.3 1.0
OE1 A:GLU213 5.0 14.5 1.0

Reference:

P.Goettig, M.Groll, J.-S.Kim, R.Huber, H.Brandstetter. Structures of the Tricorn-Interacting Aminopeptidase F1 with Different Ligands Explain Its Catalytic Mechanism Embo J. V. 21 5343 2002.
ISSN: ISSN 0261-4189
PubMed: 12374735
DOI: 10.1093/EMBOJ/CDF552
Page generated: Sat Dec 12 08:42:51 2020

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