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Calcium in PDB 8cqg: Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis

Enzymatic activity of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis

All present enzymatic activity of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis:
3.2.1.1;

Protein crystallography data

The structure of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis, PDB code: 8cqg was solved by S.Skagseth, B.A.Lund, J.J.Griese, F.Van Der Ent, J.Aqvist, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.48 / 1.74
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.879, 80.93, 128.481, 90, 90, 90
R / Rfree (%) 17.7 / 20.5

Other elements in 8cqg:

The structure of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis (pdb code 8cqg). 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 Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis, PDB code: 8cqg:

Calcium binding site 1 out of 1 in 8cqg

Go back to Calcium Binding Sites List in 8cqg
Calcium binding site 1 out of 1 in the Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis


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 Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca514

b:32.1
occ:1.00
 O A:HOH683 2.2 34.1 1.0
O A:HIS178 2.3 30.9 1.0
OD1 A:ASN88 2.4 30.9 1.0
O A:HOH762 2.5 31.9 1.0
O A:GLN135 2.5 34.1 1.0
O A:HOH679 2.5 31.8 1.0
OD2 A:ASP144 2.5 30.9 1.0
OD1 A:ASP144 2.6 34.1 1.0
CG A:ASP144 2.9 35.5 1.0
C A:GLN135 3.4 36.9 1.0
HB3 A:HIS178 3.4 38.1 1.0
C A:HIS178 3.5 29.8 1.0
HA A:GLN135 3.5 42.8 1.0
CG A:ASN88 3.5 31.5 1.0
HD21 A:ASN88 3.8 34.7 1.0
HG22 A:VAL179 3.8 39.5 1.0
HE1 A:HIS117 3.8 41.7 1.0
HD1 A:HIS117 3.9 47.5 1.0
HA A:VAL179 3.9 34.3 1.0
HA A:ASN136 4.0 40.1 1.0
CA A:GLN135 4.0 35.7 1.0
ND2 A:ASN88 4.1 28.9 1.0
CB A:HIS178 4.2 31.8 1.0
O A:ASN88 4.3 31.4 1.0
N A:ASN136 4.3 33.9 1.0
CA A:HIS178 4.3 29.4 1.0
HB2 A:HIS178 4.4 38.1 1.0
CB A:ASP144 4.4 33.9 1.0
CE1 A:HIS117 4.4 34.8 1.0
N A:VAL179 4.4 28.8 1.0
HB3 A:GLN135 4.4 44.4 1.0
ND1 A:HIS117 4.5 39.6 1.0
HG23 A:VAL179 4.5 39.5 1.0
HA A:HIS178 4.5 35.2 1.0
CG2 A:VAL179 4.5 32.9 1.0
O A:LEU145 4.6 34.2 1.0
CA A:ASN136 4.6 33.5 1.0
HA A:ASN88 4.6 33.2 1.0
CA A:VAL179 4.6 28.6 1.0
O A:CYS137 4.7 36.2 1.0
O A:VAL134 4.7 34.6 1.0
HA A:ASP144 4.8 42.0 1.0
HB3 A:ASP144 4.8 40.6 1.0
CB A:ASN88 4.8 28.2 1.0
CB A:GLN135 4.8 37.0 1.0
HB2 A:ASP144 4.9 40.6 1.0
HD22 A:ASN88 4.9 34.7 1.0
O A:HOH734 4.9 37.0 1.0
HB2 A:ASN88 5.0 33.8 1.0

Reference:

F.Van Der Ent, S.Skagseth, B.Lund, J.Socan, J.Griese, B.O.Brandsdal, J.Aqvist. Computational Design of the Temperature Optimum of An Enzyme Reaction Sci Adv 2023.
ISSN: ESSN 2375-2548
DOI: 10.1126/SCIADV.ADI0963
Page generated: Thu Jul 10 03:47:07 2025

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