Calcium in PDB 9us5: Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose

All present enzymatic activity of Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose:
3.2.1.98;

The structure of Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose, PDB code: 9us5 was solved by Z.Fujimoto, N.Kishine, M.Momma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.06 / 2.66
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	163.084, 163.084, 139.376, 90, 90, 90
R / Rfree (%)	18.2 / 22.6

The binding sites of Calcium atom in the Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose (pdb code 9us5). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose, PDB code: 9us5:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca701 b:64.4 occ:1.00 O A:GLY225 2.3 66.3 1.0 OD2 A:ASP227 2.3 59.9 1.0 OD1 A:ASP207 2.3 63.3 1.0 OD1 A:ASN206 2.3 62.3 1.0 O A:ASN203 2.4 62.9 1.0 OD1 A:ASN201 2.5 58.7 1.0 O A:HOH829 2.5 57.4 1.0 CG A:ASP227 3.3 61.9 1.0 C A:GLY225 3.4 60.9 1.0 CG A:ASN201 3.4 58.2 1.0 C A:ASN203 3.4 66.1 1.0 CG A:ASN206 3.4 61.6 1.0 CG A:ASP207 3.5 63.1 1.0 CB A:ASP227 3.8 62.4 1.0 CA A:GLY225 3.9 63.3 1.0 ND2 A:ASN206 3.9 63.8 1.0 ND2 A:ASN201 4.0 57.5 1.0 CA A:PRO204 4.1 64.2 1.0 OD2 A:ASP207 4.2 63.4 1.0 N A:PRO204 4.2 64.8 1.0 N A:ASP207 4.2 61.9 1.0 O A:ASN286 4.4 58.3 1.0 N A:ASN203 4.4 67.5 1.0 CA A:ASN203 4.4 67.7 1.0 CA A:ASP207 4.4 62.2 1.0 OD1 A:ASP227 4.4 59.8 1.0 CB A:ASN201 4.5 58.2 1.0 N A:GLY226 4.5 59.2 1.0 CA A:ASN201 4.5 58.3 1.0 CB A:ASP207 4.6 61.4 1.0 C A:ASN206 4.6 61.6 1.0 C A:PRO204 4.6 63.8 1.0 C A:GLY226 4.6 55.8 1.0 N A:ASN206 4.7 62.3 1.0 CB A:ASN206 4.7 61.0 1.0 O A:GLY226 4.7 56.4 1.0 N A:ASP227 4.8 55.0 1.0 CB A:ASN203 4.8 70.0 1.0 C A:ASN201 4.9 60.5 1.0 CA A:ASN206 4.9 61.5 1.0 CA A:GLY226 4.9 56.4 1.0 CA A:ASP227 4.9 59.2 1.0 O A:PRO204 4.9 64.4 1.0 N A:GLY202 5.0 63.8 1.0

Calcium binding site 2 out of 2 in the Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Domain N Deletion Mutant of Klebsiella Pneumoniae Maltohexaose- Producing Alpha-Amylase in Complex with Maltohexaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca702 b:81.0 occ:1.00 O A:LEU397 2.1 84.8 1.0 OD1 A:ASP406 2.4 71.9 1.0 O A:HOH811 2.4 58.2 1.0 OD1 A:ASN314 2.4 63.1 1.0 O A:HIS464 2.5 71.3 1.0 O A:HOH828 2.5 64.0 1.0 CG A:ASP406 3.1 69.2 1.0 OD2 A:ASP406 3.2 69.4 1.0 C A:LEU397 3.3 86.7 1.0 CG A:ASN314 3.6 67.4 1.0 C A:HIS464 3.7 72.1 1.0 CA A:LEU397 4.1 86.3 1.0 O A:ASN314 4.1 54.4 1.0 N A:THR398 4.2 88.5 1.0 O A:ASP396 4.3 95.3 1.0 CB A:HIS464 4.3 79.1 1.0 ND2 A:ASN314 4.4 72.5 1.0 O A:MET399 4.4 93.0 1.0 O A:LEU407 4.4 60.1 1.0 NH1 A:ARG383 4.5 69.3 1.0 CA A:HIS464 4.5 75.4 1.0 CA A:THR398 4.5 90.2 1.0 CG2 A:VAL465 4.6 63.9 1.0 CB A:ASP406 4.6 65.8 1.0 CB A:ASN314 4.7 62.8 1.0 N A:VAL465 4.7 68.6 1.0 CA A:ASN314 4.7 61.3 1.0 C A:ASN314 4.8 55.6 1.0 CA A:VAL465 4.9 64.6 1.0 C A:THR398 5.0 90.2 1.0

Z.Fujimoto, N.Kishine, M.Momma. Crystal Structure of Klebsiella Pneumoniae Maltohexaose-Producing Alpha-Amylase. J.Biochem. 2025.
ISSN: ISSN 0021-924X
PubMed: 40576559
DOI: 10.1093/JB/MVAF034