Calcium in PDB 6ag4: Crystal Structure of ARD1 N-Terminal Acetyltransferase H88A/E127A Mutant From Sulfolobus Solfataricus

Enzymatic activity of Crystal Structure of ARD1 N-Terminal Acetyltransferase H88A/E127A Mutant From Sulfolobus Solfataricus

All present enzymatic activity of Crystal Structure of ARD1 N-Terminal Acetyltransferase H88A/E127A Mutant From Sulfolobus Solfataricus:
2.3.1.255; 2.3.1.258;

Protein crystallography data

The structure of Crystal Structure of ARD1 N-Terminal Acetyltransferase H88A/E127A Mutant From Sulfolobus Solfataricus, PDB code: 6ag4 was solved by Y.Y.Chang, C.H.Hsu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.97 / 2.26
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.335, 53.148, 74.505, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 22.9

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of ARD1 N-Terminal Acetyltransferase H88A/E127A Mutant From Sulfolobus Solfataricus (pdb code 6ag4). 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 ARD1 N-Terminal Acetyltransferase H88A/E127A Mutant From Sulfolobus Solfataricus, PDB code: 6ag4:

Calcium binding site 1 out of 1 in 6ag4

Go back to Calcium Binding Sites List in 6ag4
Calcium binding site 1 out of 1 in the Crystal Structure of ARD1 N-Terminal Acetyltransferase H88A/E127A Mutant From Sulfolobus Solfataricus


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 ARD1 N-Terminal Acetyltransferase H88A/E127A Mutant From Sulfolobus Solfataricus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca203

b:53.6
occ:1.00
ND2 A:ASN132 3.0 18.0 1.0
N A:ARG129 3.3 19.9 1.0
CG A:ARG129 3.3 32.5 1.0
CB A:ARG129 3.7 24.1 1.0
C2P A:ACO201 3.7 54.5 1.0
S1P A:ACO201 3.8 65.3 1.0
CG2 A:VAL128 3.9 20.2 1.0
CD A:ARG129 3.9 36.2 1.0
CB A:ASN132 3.9 18.6 1.0
CG A:ASN132 3.9 24.0 1.0
OH A:TYR154 4.0 32.6 1.0
CA A:ARG129 4.1 23.2 1.0
CA A:VAL128 4.2 27.6 1.0
C A:VAL128 4.3 28.4 1.0
NE A:ARG129 4.4 41.4 1.0
CZ A:TYR154 4.5 31.6 1.0
CB A:VAL128 4.6 25.6 1.0
O5P A:ACO201 4.7 35.3 1.0
CE1 A:TYR154 4.8 29.8 1.0
C3P A:ACO201 4.9 33.0 1.0
C A:ACO201 4.9 62.8 1.0

Reference:

Y.Y.Chang, C.H.Hsu. Decipher the Water-Mediated Catalytic Mechanism of Thermophilic Acetyltransferase To Be Published.
Page generated: Sat Dec 12 05:56:54 2020

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