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Sodium in PDB 5i3k: Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase

Enzymatic activity of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase

All present enzymatic activity of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase:
5.3.1.1;

Protein crystallography data

The structure of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase, PDB code: 5i3k was solved by E.J.Drake, A.M.Gulick, J.P.Richard, X.Zhai, K.Kim, C.J.Reinhardt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.91 / 2.21
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.890, 87.600, 76.380, 90.00, 107.35, 90.00
R / Rfree (%) 21.9 / 26.4

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase (pdb code 5i3k). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase, PDB code: 5i3k:
Jump to Sodium binding site number: 1; 2; 3;

Sodium binding site 1 out of 3 in 5i3k

Go back to Sodium Binding Sites List in 5i3k
Sodium binding site 1 out of 3 in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:33.0
occ:1.00
O A:HOH469 2.4 22.4 1.0
O A:HOH429 2.4 30.4 1.0
O A:ALA160 3.4 25.5 1.0
CA A:ALA160 3.8 23.9 1.0
C A:ALA160 4.0 23.5 1.0
O A:HOH432 4.1 22.2 1.0
O A:GLU205 4.3 23.0 1.0
CB A:ALA160 4.4 22.7 1.0
OE1 A:GLU205 4.4 45.3 1.0
NE A:ARG207 4.4 19.8 1.0
NH2 A:ARG207 4.5 28.9 1.0
O A:TRP159 4.6 27.2 1.0
CB A:GLU205 4.6 25.5 1.0
CZ A:ARG207 4.6 23.9 1.0
O A:HOH454 4.6 20.5 1.0
N A:ALA160 4.9 24.3 1.0
C A:GLU205 5.0 21.6 1.0

Sodium binding site 2 out of 3 in 5i3k

Go back to Sodium Binding Sites List in 5i3k
Sodium binding site 2 out of 3 in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na302

b:37.1
occ:1.00
O A:HOH473 2.5 42.4 1.0
O A:HOH497 2.6 51.5 1.0
O A:HOH495 3.9 35.4 1.0
O A:PRO58 3.9 24.9 1.0
C A:PRO58 4.7 25.5 1.0
O A:HOH418 4.7 31.0 1.0

Sodium binding site 3 out of 3 in 5i3k

Go back to Sodium Binding Sites List in 5i3k
Sodium binding site 3 out of 3 in the Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Structure-Function Studies on Role of Hydrophobic Clamping of A Basic Glutamate in Catalysis By Triosephosphate Isomerase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na302

b:39.9
occ:1.00
O C:HOH479 2.4 26.8 1.0
CZ C:PHE74 3.7 19.4 1.0
CB C:LYS70 3.8 29.6 1.0
O C:HOH507 3.9 27.8 1.0
CE2 C:PHE74 4.0 23.4 1.0
N C:LYS70 4.3 25.8 1.0
CA C:LYS70 4.6 27.7 1.0
O C:LYS70 4.6 26.9 1.0
CE1 C:PHE74 4.6 23.1 1.0
C C:LYS70 4.9 24.9 1.0
CB C:ALA69 4.9 27.8 1.0

Reference:

J.P.Richard, T.L.Amyes, M.M.Malabanan, X.Zhai, K.J.Kim, C.J.Reinhardt, R.K.Wierenga, E.J.Drake, A.M.Gulick. Structure-Function Studies of Hydrophobic Residues That Clamp A Basic Glutamate Side Chain During Catalysis By Triosephosphate Isomerase. Biochemistry V. 55 3036 2016.
ISSN: ISSN 0006-2960
PubMed: 27149328
DOI: 10.1021/ACS.BIOCHEM.6B00311
Page generated: Tue Dec 15 11:04:08 2020

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