Atomistry » Calcium » PDB 1ukg-1ux6 » 1uks
Atomistry »
  Calcium »
    PDB 1ukg-1ux6 »
      1uks »

Calcium in PDB 1uks: Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose

Enzymatic activity of Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose

All present enzymatic activity of Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose:
2.4.1.19;

Protein crystallography data

The structure of Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose, PDB code: 1uks was solved by K.Haga, R.Kanai, O.Sakamoto, K.Harata, K.Yamane, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 64.850, 74.530, 78.940, 85.19, 104.86, 101.04
R / Rfree (%) 16.2 / 21.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose (pdb code 1uks). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose, PDB code: 1uks:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in 1uks

Go back to Calcium Binding Sites List in 1uks
Calcium binding site 1 out of 4 in the Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From 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 F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca687

b:12.4
occ:1.00
 OD1 A:ASN33 2.1 11.9 1.0
OD1 A:ASN32 2.2 14.6 1.0
O A:HOH1001 2.2 10.8 1.0
O A:GLY51 2.3 11.6 1.0
O A:ASN29 2.3 17.1 1.0
OD2 A:ASP53 2.5 11.6 1.0
OD2 A:ASP27 2.5 12.4 1.0
CG A:ASN33 3.4 12.8 1.0
CG A:ASN32 3.4 10.1 1.0
CG A:ASP27 3.5 11.1 1.0
C A:GLY51 3.5 9.9 1.0
C A:ASN29 3.5 15.2 1.0
CG A:ASP53 3.5 10.7 1.0
CB A:ASP53 3.9 11.0 1.0
CA A:GLY51 4.0 8.6 1.0
OD1 A:ASP27 4.0 9.8 1.0
ND2 A:ASN32 4.1 9.9 1.0
O A:ALA111 4.1 14.1 1.0
N A:ASN33 4.1 13.6 1.0
ND2 A:ASN33 4.2 13.4 1.0
N A:PRO30 4.2 15.8 1.0
CA A:ASN33 4.3 15.5 1.0
CA A:PRO30 4.3 17.0 1.0
N A:ASN29 4.3 15.4 1.0
C A:ASN32 4.4 12.0 1.0
CA A:ASN29 4.4 14.6 1.0
CB A:ASN33 4.4 12.9 1.0
CB A:ASP27 4.4 11.1 1.0
OD1 A:ASP53 4.5 8.9 1.0
CA A:ASP27 4.5 12.4 1.0
N A:GLY52 4.6 11.7 1.0
CB A:ASN32 4.6 12.1 1.0
C A:GLY52 4.7 9.1 1.0
O A:HOH1074 4.7 14.5 1.0
C A:PRO30 4.7 16.4 1.0
O A:ASN32 4.7 11.6 1.0
N A:ASN32 4.7 12.1 1.0
CA A:ASN32 4.8 10.6 1.0
CB A:ASN29 4.8 17.1 1.0
O A:PRO30 4.8 17.0 1.0
N A:ASP53 4.8 9.4 1.0
O A:GLY52 4.8 10.0 1.0
CA A:GLY52 5.0 9.8 1.0

Calcium binding site 2 out of 4 in 1uks

Go back to Calcium Binding Sites List in 1uks
Calcium binding site 2 out of 4 in the Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca688

b:36.3
occ:1.00
 O A:HOH1004 2.2 19.8 1.0
O A:ILE190 2.3 9.8 1.0
O A:HOH1003 2.3 17.3 1.0
O A:HOH1002 2.4 26.1 1.0
O A:HIS233 2.4 12.7 1.0
OD1 A:ASN139 2.4 16.5 1.0
OD1 A:ASP199 2.9 25.9 1.0
C A:ILE190 3.4 13.2 1.0
CG A:ASN139 3.6 13.1 1.0
C A:HIS233 3.7 12.0 1.0
CG A:ASP199 3.7 21.9 1.0
CA A:ILE190 4.0 12.5 1.0
ND2 A:ASN139 4.0 15.7 1.0
OD2 A:ASP199 4.0 20.1 1.0
O A:GLY189 4.4 12.7 1.0
ND1 A:HIS176 4.4 14.0 1.0
CE1 A:HIS176 4.5 14.1 1.0
N A:MET234 4.5 10.4 1.0
CA A:MET234 4.5 11.8 1.0
N A:TYR191 4.6 13.7 1.0
CG2 A:ILE190 4.6 9.8 1.0
CB A:HIS233 4.6 11.4 1.0
CA A:HIS233 4.6 13.7 1.0
O A:ASN139 4.7 12.0 1.0
CG A:MET234 4.7 10.5 1.0
O A:LYS192 4.7 21.3 1.0
CB A:ASP199 4.8 18.0 1.0
CA A:TYR191 4.8 12.9 1.0
CB A:ASN139 4.9 10.4 1.0
CB A:ILE190 4.9 12.3 1.0
O A:HOH1239 5.0 26.7 1.0

Calcium binding site 3 out of 4 in 1uks

Go back to Calcium Binding Sites List in 1uks
Calcium binding site 3 out of 4 in the Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca689

b:15.6
occ:1.00
 OD1 B:ASN33 2.1 17.3 1.0
O B:HOH1169 2.2 19.3 1.0
OD1 B:ASN32 2.2 16.3 1.0
O B:GLY51 2.2 15.1 1.0
O B:ASN29 2.3 20.4 1.0
OD2 B:ASP27 2.4 15.6 1.0
OD2 B:ASP53 2.5 15.3 1.0
CG B:ASN33 3.4 16.8 1.0
C B:GLY51 3.4 13.8 1.0
CG B:ASP27 3.4 16.3 1.0
CG B:ASN32 3.4 13.5 1.0
CG B:ASP53 3.4 14.6 1.0
C B:ASN29 3.5 17.1 1.0
CB B:ASP53 3.9 12.1 1.0
CA B:GLY51 3.9 13.5 1.0
ND2 B:ASN32 4.1 17.0 1.0
ND2 B:ASN33 4.1 17.2 1.0
OD1 B:ASP27 4.1 18.0 1.0
N B:ASN33 4.2 16.0 1.0
N B:PRO30 4.2 18.9 1.0
O B:ALA111 4.2 13.7 1.0
CA B:PRO30 4.2 20.8 1.0
N B:ASN29 4.3 16.5 1.0
CA B:ASN33 4.4 17.7 1.0
CB B:ASP27 4.4 14.8 1.0
CA B:ASN29 4.4 17.4 1.0
OD1 B:ASP53 4.4 13.7 1.0
C B:ASN32 4.4 14.5 1.0
CB B:ASN33 4.5 16.5 1.0
CA B:ASP27 4.5 15.4 1.0
N B:GLY52 4.5 13.3 1.0
CB B:ASN32 4.7 16.9 1.0
C B:GLY52 4.7 12.2 1.0
O B:HOH1070 4.7 16.3 1.0
CB B:ASN29 4.7 17.7 1.0
O B:ASN32 4.8 17.0 1.0
C B:PRO30 4.8 19.4 1.0
N B:ASP53 4.8 10.9 1.0
N B:ASN32 4.9 17.8 1.0
O B:GLY52 4.9 12.1 1.0
CA B:GLY52 4.9 12.7 1.0
C B:ASP27 4.9 15.4 1.0
CA B:ASN32 4.9 16.1 1.0
O B:PRO30 4.9 20.8 1.0
N B:GLY28 5.0 15.0 1.0

Calcium binding site 4 out of 4 in 1uks

Go back to Calcium Binding Sites List in 1uks
Calcium binding site 4 out of 4 in the Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Crystal Structure of F183L/F259L Mutant Cyclodextrin Glucanotransferase Complexed with A Pseudo-Maltotetraose Derived From Acarbose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca690

b:34.2
occ:1.00
 O B:HOH1069 2.2 14.1 1.0
OD1 B:ASN139 2.2 16.0 1.0
O B:HOH1005 2.3 18.5 1.0
O B:HIS233 2.4 12.9 1.0
O B:HOH1314 2.4 30.1 1.0
O B:ILE190 2.5 14.1 1.0
O B:HOH1006 3.0 38.2 1.0
CG B:ASN139 3.3 14.2 1.0
OD1 B:ASP199 3.6 29.3 1.0
C B:ILE190 3.6 16.4 1.0
C B:HIS233 3.6 14.0 1.0
ND2 B:ASN139 3.7 16.8 1.0
CA B:ILE190 4.1 17.0 1.0
CG B:ASP199 4.2 25.6 1.0
O B:GLY189 4.4 15.3 1.0
CB B:HIS233 4.4 12.7 1.0
CA B:MET234 4.5 12.2 1.0
N B:MET234 4.5 12.8 1.0
CA B:HIS233 4.5 12.8 1.0
CB B:ASP199 4.5 21.0 1.0
ND1 B:HIS176 4.6 16.4 1.0
O B:ASN139 4.6 19.3 1.0
CG B:MET234 4.7 14.3 1.0
O B:LYS192 4.7 22.8 1.0
CB B:ASN139 4.7 13.8 1.0
N B:TYR191 4.7 16.8 1.0
CG2 B:ILE190 4.7 13.6 1.0
CE1 B:HIS176 4.8 15.7 1.0
OD2 B:ASP199 4.9 25.7 1.0

Reference:

K.Haga, R.Kanai, O.Sakamoto, M.Aoyagi, K.Harata, K.Yamane. Effects of Essential Carbohydrate/Aromatic Stacking Interaction with TYR100 and PHE259 on Substrate Binding of Cyclodextrin Glycosyltransferase From Alkalophilic Bacillus Sp. 1011 J.Biochem.(Tokyo) V. 134 881 2003.
ISSN: ISSN 0021-924X
PubMed: 14769878
DOI: 10.1093/JB/MVG215
Page generated: Thu Jul 11 23:31:40 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy