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Sodium in PDB 7cm8: High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae

Enzymatic activity of High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae

All present enzymatic activity of High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae:
2.5.1.47;

Protein crystallography data

The structure of High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae, PDB code: 7cm8 was solved by A.Kaushik, R.Rahisuddin, N.Saini, S.Kumaran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.56 / 1.90
Space group I 41
Cell size a, b, c (Å), α, β, γ (°) 112.440, 112.440, 44.000, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 23.1

Sodium Binding Sites:

The binding sites of Sodium atom in the High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae (pdb code 7cm8). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 5 binding sites of Sodium where determined in the High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae, PDB code: 7cm8:
Jump to Sodium binding site number: 1; 2; 3; 4; 5;

Sodium binding site 1 out of 5 in 7cm8

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Sodium binding site 1 out of 5 in the High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na401

b:39.1
occ:1.00
OH A:TYR305 2.5 26.0 1.0
O A:GLN227 2.8 23.0 1.0
N A:SER272 2.9 20.8 1.0
CZ A:TYR305 3.1 29.8 1.0
OG A:SER272 3.1 21.2 1.0
C2' A:LLP42 3.1 24.4 1.0
CB A:SER272 3.2 19.6 1.0
CE1 A:TYR305 3.3 26.3 1.0
NA A:NA406 3.5 31.4 1.0
N A:ILE271 3.5 24.4 1.0
CA A:SER272 3.6 19.8 1.0
C A:ILE271 3.8 21.0 1.0
C A:GLN227 3.8 26.9 1.0
OG A:SER300 3.9 34.5 1.0
CA A:ILE271 4.0 24.0 1.0
CB A:ILE271 4.0 25.2 1.0
C A:GLY270 4.1 26.0 1.0
CE2 A:TYR305 4.2 27.2 1.0
C2 A:LLP42 4.3 21.5 1.0
CB A:GLN227 4.4 26.9 1.0
CA A:GLY270 4.5 26.2 1.0
CA A:GLN227 4.5 26.9 1.0
CD1 A:TYR305 4.5 24.1 1.0
N A:GLN227 4.5 26.6 1.0
N1 A:LLP42 4.5 22.6 1.0
C A:SER272 4.8 17.9 1.0
N A:SER273 4.8 20.0 1.0
N A:GLY228 4.9 28.2 1.0
O A:GLY270 4.9 24.2 1.0
CG2 A:ILE271 4.9 27.6 1.0
O A:ILE271 4.9 25.4 1.0

Sodium binding site 2 out of 5 in 7cm8

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Sodium binding site 2 out of 5 in the High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na402

b:24.2
occ:1.00
N A:VAL28 2.9 21.3 1.0
O A:PHE22 2.9 24.9 1.0
CA A:GLY26 3.0 26.7 1.0
C A:GLY26 3.0 27.8 1.0
N A:ASN27 3.1 25.0 1.0
O A:HOH558 3.1 26.5 1.0
O A:LEU19 3.2 22.4 1.0
O A:VAL28 3.3 21.7 1.0
N A:GLY26 3.5 26.4 1.0
CB A:VAL28 3.6 19.3 1.0
CA A:VAL28 3.6 21.6 1.0
O A:GLY26 3.7 33.0 1.0
CA A:GLY23 3.8 22.8 1.0
C A:PHE22 3.9 23.2 1.0
OD1 A:ASN27 3.9 23.4 1.0
C A:ASN27 3.9 24.5 1.0
C A:VAL28 3.9 23.1 1.0
CG2 A:VAL28 4.0 22.3 1.0
CA A:ASN27 4.0 24.5 1.0
C A:LEU19 4.1 27.0 1.0
N A:HIS24 4.2 21.8 1.0
C A:GLY23 4.2 24.8 1.0
CB A:LEU19 4.2 24.6 1.0
N A:GLY23 4.3 23.4 1.0
N A:LEU19 4.4 23.6 1.0
CA A:LEU19 4.5 25.1 1.0
C A:ASN25 4.8 27.9 1.0
CG A:ASN27 4.8 24.9 1.0
CG A:ARG18 4.9 26.2 1.0
CB A:ASN27 4.9 23.9 1.0
CG1 A:VAL28 5.0 18.4 1.0
O A:HIS24 5.0 23.4 1.0

Sodium binding site 3 out of 5 in 7cm8

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Sodium binding site 3 out of 5 in the High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na404

b:21.9
occ:1.00
OP2 A:LLP42 2.7 25.5 1.0
N A:ILE182 2.8 23.2 1.0
O A:GLY175 3.2 16.8 1.0
N A:SER181 3.4 26.1 1.0
O A:GLY179 3.5 18.4 1.0
CB A:SER181 3.5 28.8 1.0
C A:GLY179 3.6 18.0 1.0
CG2 A:ILE182 3.6 24.6 1.0
CB A:ILE182 3.6 25.7 1.0
P A:LLP42 3.6 24.2 1.0
OP3 A:LLP42 3.6 16.8 1.0
CA A:GLY179 3.6 18.1 1.0
C A:SER181 3.7 25.9 1.0
CA A:SER181 3.7 24.9 1.0
CA A:ILE182 3.7 25.6 1.0
CG2 A:VAL176 3.9 21.8 1.0
CA A:VAL176 4.1 19.4 1.0
N A:GLY179 4.1 20.0 1.0
N A:GLY180 4.1 22.4 1.0
CB A:ALA174 4.2 15.3 1.0
OP4 A:LLP42 4.2 25.5 1.0
OG A:SER181 4.2 27.9 1.0
C A:GLY175 4.2 18.7 1.0
C A:GLY180 4.3 24.6 1.0
O A:HOH560 4.4 23.4 1.0
CB A:VAL176 4.5 19.6 1.0
N A:VAL176 4.6 17.6 1.0
O A:ALA174 4.8 15.3 1.0
O A:HOH548 4.8 26.7 1.0
CA A:GLY180 4.8 26.3 1.0
N A:THR183 4.8 21.6 1.0
C A:ILE182 4.9 24.2 1.0
O A:SER181 4.9 24.0 1.0
C5' A:LLP42 4.9 26.8 1.0
C A:ALA174 4.9 13.8 1.0
OP1 A:LLP42 4.9 17.6 1.0
N A:GLY177 4.9 21.9 1.0
CG1 A:VAL176 4.9 20.5 1.0

Sodium binding site 4 out of 5 in 7cm8

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Sodium binding site 4 out of 5 in the High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 4 of High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na406

b:31.4
occ:1.00
OG A:SER272 2.6 21.2 1.0
OG A:SER300 2.9 34.5 1.0
OG A:SER273 2.9 25.5 1.0
N A:SER273 3.0 20.0 1.0
N A:SER300 3.3 22.2 1.0
CB A:SER273 3.3 24.6 1.0
CA A:GLY270 3.4 26.2 1.0
C A:GLY270 3.5 26.0 1.0
NA A:NA401 3.5 39.1 1.0
N A:SER272 3.5 20.8 1.0
N A:GLY270 3.6 25.9 1.0
CD A:PRO299 3.6 21.4 1.0
CB A:SER272 3.7 19.6 1.0
O A:GLY270 3.7 24.2 1.0
CA A:SER273 3.7 21.2 1.0
C A:SER272 3.7 17.9 1.0
CA A:SER272 3.8 19.8 1.0
CB A:PRO299 3.9 19.8 1.0
CB A:SER300 3.9 26.6 1.0
N A:PRO299 3.9 18.2 1.0
OH A:TYR305 4.0 26.0 1.0
CG A:PRO299 4.0 22.1 1.0
CA A:SER300 4.0 24.1 1.0
N A:ILE271 4.1 24.4 1.0
C2' A:LLP42 4.1 24.4 1.0
C A:PRO299 4.2 21.4 1.0
O A:SER300 4.2 20.5 1.0
CA A:PRO299 4.2 21.0 1.0
C A:SER300 4.3 22.8 1.0
C A:ILE271 4.4 21.0 1.0
C A:LEU298 4.6 18.4 1.0
CZ A:TYR305 4.7 29.8 1.0
O A:SER272 4.7 17.8 1.0
N1 A:LLP42 4.8 22.6 1.0
C A:ALA269 4.8 26.0 1.0
CA A:ILE271 4.9 24.0 1.0
CE2 A:TYR305 4.9 27.2 1.0
C2 A:LLP42 4.9 21.5 1.0

Sodium binding site 5 out of 5 in 7cm8

Go back to Sodium Binding Sites List in 7cm8
Sodium binding site 5 out of 5 in the High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 5 of High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na407

b:35.4
occ:1.00
O A:HOH541 2.5 17.9 1.0
O A:SER272 2.7 17.8 1.0
CA A:GLY175 3.3 16.7 1.0
C A:SER272 3.4 17.9 1.0
N A:GLY175 3.5 16.2 1.0
CB A:SER272 3.6 19.6 1.0
CG2 A:ILE229 3.8 24.3 1.0
OG A:SER272 3.8 21.2 1.0
CB A:ALA276 3.9 21.3 1.0
CG A:PRO299 3.9 22.1 1.0
CA A:SER272 3.9 19.8 1.0
CD A:PRO299 4.1 21.4 1.0
N A:ALA276 4.1 20.7 1.0
C A:GLY175 4.3 18.7 1.0
C6 A:LLP42 4.4 21.8 1.0
O A:HOH560 4.4 23.4 1.0
N A:SER273 4.4 20.0 1.0
O A:ILE297 4.5 14.5 1.0
CA A:ALA276 4.5 23.1 1.0
N1 A:LLP42 4.5 22.6 1.0
O A:GLY175 4.7 16.8 1.0
CD1 A:ILE229 4.7 23.1 1.0
C A:ALA174 4.7 13.8 1.0
CB A:ALA275 4.8 26.0 1.0
CA A:SER273 4.9 21.2 1.0

Reference:

A.Kaushik, R.Rahisuddin, N.Saini, S.Kumaran. High Resolution Crystal Structure of M92A Mutant of O-Acetyl-L-Serine Sulfhydrylase From Haemophilus Influenzae To Be Published.
Page generated: Tue Oct 8 16:23:22 2024

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