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Calcium in PDB 8cqf: Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis Complexed with Rearranged Acarbose

Enzymatic activity of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis Complexed with Rearranged Acarbose

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

Protein crystallography data

The structure of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis Complexed with Rearranged Acarbose, PDB code: 8cqf was solved by S.Skagseth, J.J.Griese, B.A.Lund, 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) 38.69 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 68.597, 81.071, 129.534, 90, 90, 90
R / Rfree (%) 16.9 / 19.8

Other elements in 8cqf:

The structure of Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis Complexed with Rearranged Acarbose 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 Complexed with Rearranged Acarbose (pdb code 8cqf). 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 Complexed with Rearranged Acarbose, PDB code: 8cqf:

Calcium binding site 1 out of 1 in 8cqf

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


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 Complexed with Rearranged Acarbose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca503

b:30.7
occ:1.00
 O A:HOH747 2.3 31.6 1.0
O A:HOH648 2.3 30.5 1.0
O A:HIS178 2.4 32.2 1.0
OD1 A:ASN88 2.4 29.5 1.0
O A:HOH741 2.4 32.7 1.0
OD2 A:ASP144 2.4 33.3 1.0
O A:GLN135 2.5 33.9 1.0
OD1 A:ASP144 2.6 32.3 1.0
CG A:ASP144 2.8 38.5 1.0
HB3 A:HIS178 3.4 34.9 1.0
C A:GLN135 3.4 38.1 1.0
CG A:ASN88 3.5 32.0 1.0
C A:HIS178 3.5 34.3 1.0
HA A:GLN135 3.5 47.8 1.0
HG22 A:VAL179 3.6 50.2 1.0
HD21 A:ASN88 3.6 37.3 1.0
HD1 A:HIS117 3.9 47.3 1.0
HA A:VAL179 3.9 41.2 1.0
HA A:ASN136 3.9 49.8 1.0
HE1 A:HIS117 4.0 52.7 1.0
ND2 A:ASN88 4.0 31.0 1.0
CA A:GLN135 4.0 39.8 1.0
CB A:HIS178 4.1 29.0 1.0
HB2 A:HIS178 4.3 34.9 1.0
O A:ASN88 4.3 30.5 1.0
N A:ASN136 4.3 34.5 1.0
CA A:HIS178 4.3 34.0 1.0
CB A:ASP144 4.4 33.7 1.0
CG2 A:VAL179 4.4 41.8 1.0
HG23 A:VAL179 4.4 50.2 1.0
N A:VAL179 4.4 32.4 1.0
HB3 A:GLN135 4.4 39.9 1.0
ND1 A:HIS117 4.5 39.4 1.0
CE1 A:HIS117 4.5 43.9 1.0
HA A:HIS178 4.5 40.9 1.0
CA A:ASN136 4.6 41.5 1.0
HA A:ASN88 4.6 38.2 1.0
CA A:VAL179 4.6 34.3 1.0
O A:LEU145 4.6 33.3 1.0
O A:CYS137 4.7 39.7 1.0
CB A:ASN88 4.7 29.0 1.0
HB3 A:ASP144 4.7 40.4 1.0
HA A:ASP144 4.7 46.0 1.0
O A:VAL134 4.7 35.7 1.0
HD22 A:ASN88 4.8 37.3 1.0
HB2 A:ASP144 4.8 40.4 1.0
CB A:GLN135 4.9 33.2 1.0
HB2 A:ASN88 4.9 34.8 1.0
O A:HOH699 5.0 37.0 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 03:46:49 2025

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