Chlorine 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:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of A Chimeric Alpha-Amylase From Pseudoalteromonas Haloplanktis Complexed with Rearranged Acarbose, PDB code: 8cqf:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 8cqf

Go back to Chlorine Binding Sites List in 8cqf
Chlorine binding site 1 out of 2 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 Chlorine with other atoms in the Cl 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:Cl501

b:31.4
occ:1.00
 HH22 A:ARG301 2.4 41.6 1.0
HD22 A:ASN262 2.5 37.7 1.0
HE A:ARG172 2.5 37.9 1.0
HH21 A:ARG172 2.5 41.5 1.0
HH12 A:ARG301 2.6 35.0 1.0
HG3 A:GLU200 3.1 37.9 1.0
HG21 A:THR221 3.1 39.4 1.0
NH2 A:ARG301 3.2 34.7 1.0
NH2 A:ARG172 3.3 34.6 1.0
NE A:ARG172 3.3 31.6 1.0
ND2 A:ASN262 3.3 31.4 1.0
O A:HOH813 3.3 27.4 1.0
HZ A:PHE223 3.4 40.3 1.0
NH1 A:ARG301 3.4 29.2 1.0
HD21 A:ASN262 3.6 37.7 1.0
CZ A:ARG172 3.7 32.6 1.0
CZ A:ARG301 3.7 29.8 1.0
HH21 A:ARG301 3.8 41.6 1.0
HG22 A:THR221 3.9 39.4 1.0
HB2 A:ASN262 3.9 30.4 1.0
CG2 A:THR221 3.9 32.8 1.0
HH22 A:ARG172 3.9 41.5 1.0
CG A:GLU200 4.0 31.6 1.0
HB2 A:GLU200 4.0 33.7 1.0
CZ A:PHE223 4.1 33.6 1.0
HH11 A:ARG301 4.1 35.0 1.0
HB3 A:ASN262 4.3 30.4 1.0
HD2 A:ARG172 4.3 38.4 1.0
CG A:ASN262 4.3 31.0 1.0
CB A:ASN262 4.4 25.4 1.0
CD A:ARG172 4.4 32.0 1.0
HE1 A:PHE223 4.4 34.4 1.0
HG2 A:GLU200 4.5 37.9 1.0
HG23 A:THR221 4.5 39.4 1.0
HZ A:PHE259 4.5 37.8 1.0
CB A:GLU200 4.6 28.1 1.0
HE1 A:HIS263 4.6 39.7 1.0
HB A:THR221 4.6 35.7 1.0
CE1 A:PHE223 4.7 28.7 1.0
CZ A:PHE259 4.7 31.5 1.0
HE2 A:PHE198 4.7 34.2 1.0
HE2 A:PHE259 4.7 35.8 1.0
HE22 A:GLN33 4.7 31.5 1.0
O A:HOH655 4.7 27.1 1.0
CE2 A:PHE259 4.8 29.9 1.0
HA A:GLU200 4.8 34.9 1.0
CD A:GLU200 4.8 36.8 1.0
CB A:THR221 4.9 29.7 1.0
OE2 A:GLU200 4.9 41.5 1.0
HG3 A:ARG172 4.9 35.0 1.0
HE2 A:PHE223 4.9 39.0 1.0
CE2 A:PHE223 4.9 32.5 1.0
O A:HOH692 5.0 40.6 1.0

Chlorine binding site 2 out of 2 in 8cqf

Go back to Chlorine Binding Sites List in 8cqf
Chlorine binding site 2 out of 2 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 Chlorine with other atoms in the Cl binding site number 2 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:Cl502

b:42.3
occ:1.00
 H A:LEU57 2.3 36.3 1.0
HH11 A:ARG64 2.4 35.0 1.0
HD2 A:ARG64 2.7 38.7 1.0
HA A:GLU56 2.8 42.2 1.0
O A:HOH885 3.1 40.0 1.0
N A:LEU57 3.1 30.2 1.0
NH1 A:ARG64 3.2 29.1 1.0
HG A:LEU57 3.4 36.6 1.0
HB3 A:GLU56 3.5 40.3 1.0
HH12 A:ARG64 3.5 35.0 1.0
HB2 A:LEU57 3.6 34.5 1.0
CA A:GLU56 3.6 35.2 1.0
CD A:ARG64 3.6 32.3 1.0
HB2 A:ARG64 3.8 35.8 1.0
C A:GLU56 3.9 34.1 1.0
HD3 A:ARG64 4.0 38.7 1.0
CB A:GLU56 4.0 33.6 1.0
CZ A:ARG64 4.1 35.4 1.0
CB A:LEU57 4.1 28.7 1.0
HG2 A:GLU56 4.1 45.6 1.0
CA A:LEU57 4.2 27.9 1.0
CG A:LEU57 4.2 30.5 1.0
NE A:ARG64 4.3 32.0 1.0
CG A:ARG64 4.5 32.4 1.0
HG3 A:ARG64 4.5 38.9 1.0
CB A:ARG64 4.6 29.8 1.0
O A:TYR55 4.6 36.0 1.0
CG A:GLU56 4.7 38.0 1.0
HD12 A:LEU57 4.7 39.1 1.0
N A:GLU56 4.8 29.9 1.0
HB2 A:GLU56 4.9 40.3 1.0
O A:HOH754 4.9 32.2 1.0
C A:LEU57 4.9 30.8 1.0
HA A:LEU57 4.9 33.5 1.0
HB3 A:ARG64 4.9 35.8 1.0
O A:HOH615 5.0 41.9 1.0
HD23 A:LEU57 5.0 40.0 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: Wed Jul 26 15:56:46 2023

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