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Chlorine in PDB 1lyv: High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate.

Enzymatic activity of High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate.

All present enzymatic activity of High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate.:
3.1.3.48;

Protein crystallography data

The structure of High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate., PDB code: 1lyv was solved by A.G.Evdokimov, D.S.Waugh, K.Routzahn, J.Tropea, S.Cherry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.36
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.456, 49.331, 97.537, 90.00, 90.00, 90.00
R / Rfree (%) 12.9 / 19

Chlorine Binding Sites:

The binding sites of Chlorine atom in the High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate. (pdb code 1lyv). 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 High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate., PDB code: 1lyv:

Chlorine binding site 1 out of 1 in 1lyv

Go back to Chlorine Binding Sites List in 1lyv
Chlorine binding site 1 out of 1 in the High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl999

b:29.0
occ:1.00
 O A:ARG216 2.8 14.0 1.0
CG A:GLN237 2.8 32.1 1.0
NE A:ARG235 3.0 13.4 1.0
N A:GLN237 3.0 13.0 1.0
NH1 A:ARG236 3.2 50.1 0.5
N A:ARG236 3.3 11.0 1.0
OE1 A:GLN237 3.4 30.7 1.0
CD A:GLN237 3.4 35.1 1.0
CB A:GLN237 3.5 19.0 1.0
CD A:ARG235 3.5 11.8 1.0
CG A:ARG235 3.5 10.3 1.0
C A:ARG216 3.5 12.3 1.0
CA A:ARG216 3.7 13.4 1.0
CA A:GLN237 3.8 16.2 1.0
CA A:ARG236 3.8 11.4 1.0
CB A:ARG236 3.8 13.6 1.0
C A:ARG236 3.9 11.0 1.0
CZ A:ARG235 3.9 15.2 1.0
CZ A:ARG236 4.0 30.4 0.5
C A:ARG235 4.1 9.9 1.0
NH2 A:ARG235 4.2 18.2 1.0
NH2 A:ARG236 4.3 35.5 0.5
CB A:ARG216 4.3 15.1 1.0
NE2 A:GLN237 4.5 33.2 1.0
O A:PRO215 4.5 15.4 1.0
CA A:ARG235 4.5 10.0 1.0
CB A:ARG235 4.6 10.9 1.0
N A:TYR217 4.7 12.4 1.0
NE A:ARG236 4.9 24.0 0.5
CG A:ARG236 4.9 18.1 1.0
N A:ARG216 4.9 14.5 1.0
O A:ARG235 5.0 11.5 1.0
CG A:ARG216 5.0 15.8 1.0

Reference:

A.G.Evdokimov, D.S.Waugh, K.Routzahn, J.Tropea, S.Cherry. High-Resolution Structure of the Catalytically Inactive Yersinia Tyrosine Phosphatase C403A Mutant in Complex with Phosphate. To Be Published.
Page generated: Fri Jul 19 23:59:24 2024

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