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Calcium in PDB 3pf3: Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts

Enzymatic activity of Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts

All present enzymatic activity of Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts:
5.3.1.1;

Protein crystallography data

The structure of Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts, PDB code: 3pf3 was solved by S.Enriquez-Flores, A.Rodriguez-Romero, A.Hernandez-Santoyo, H.Reyes-Vivas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.90 / 2.10
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 56.373, 102.881, 118.908, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 20.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts (pdb code 3pf3). 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 A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts, PDB code: 3pf3:

Calcium binding site 1 out of 1 in 3pf3

Go back to Calcium Binding Sites List in 3pf3
Calcium binding site 1 out of 1 in the Crystal Structure of A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts


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 A Mutant (C202A) of Triosephosphate Isomerase From Giardia Lamblia Derivatized with Mmts within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca260

b:39.4
occ:1.00
 OE1 A:GLU170 3.0 35.0 1.0
O A:HOH291 3.1 34.8 1.0
NE2 A:HIS96 3.4 28.8 1.0
OE2 A:GLU170 3.5 31.4 1.0
CD A:GLU170 3.6 36.5 1.0
ND2 A:ASN11 3.7 23.9 1.0
CE A:LYS13 3.9 32.6 1.0
CG A:LEU235 3.9 20.8 1.0
CD2 A:HIS96 4.0 24.1 1.0
CB A:ASN11 4.0 16.6 1.0
CA A:GLY237 4.1 23.3 1.0
N A:GLY237 4.1 25.0 1.0
CD2 A:LEU235 4.2 23.9 1.0
NZ A:LYS13 4.3 28.3 1.0
O A:LEU235 4.4 20.8 1.0
C A:VAL236 4.4 24.0 1.0
CG A:ASN11 4.4 21.6 1.0
CE1 A:HIS96 4.5 32.1 1.0
O A:VAL236 4.5 19.7 1.0
C A:LEU235 4.6 25.2 1.0
CD1 A:LEU235 4.8 19.6 1.0
N A:VAL236 4.9 19.4 1.0
CB A:LEU235 4.9 16.5 1.0
O1 A:SO4259 4.9 33.5 1.0

Reference:

S.Enriquez-Flores, A.Rodriguez-Romero, G.Hernandez-Alcantara, J.Oria-Hernandez, P.Gutierrez-Castrellon, G.Perez-Hernandez, L.Mora-Ide, A.Castillo-Villanueva, I.Garcia-Torres, S.T.Mendez, S.Gomez-Manzo, A.Torres-Arroyo, G.Lopez-Velazquez, H.Reyes-Vivas. Determining the Molecular Mechanism of Inactivation By Chemical Modification of Triosephosphate Isomerase From the Human Parasite Giardia Lamblia: A Study For Antiparasitic Drug Design. Proteins V. 79 2711 2011.
ISSN: ISSN 0887-3585
PubMed: 21786322
DOI: 10.1002/PROT.23100
Page generated: Sat Jul 13 16:49:22 2024

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