Atomistry » Calcium » PDB 4llt-4m17 » 4lpl
Atomistry »
  Calcium »
    PDB 4llt-4m17 »
      4lpl »

Calcium in PDB 4lpl: Structure of CBM32-1 From A Family 31 Glycoside Hydrolase From Clostridium Perfringens

Protein crystallography data

The structure of Structure of CBM32-1 From A Family 31 Glycoside Hydrolase From Clostridium Perfringens, PDB code: 4lpl was solved by J.M.Grondin, D.Duan, F.S.Heather, C.A.Spencer, J.S.Allingham, S.P.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.64 / 1.35
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 55.620, 55.671, 88.700, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 20.7

Other elements in 4lpl:

The structure of Structure of CBM32-1 From A Family 31 Glycoside Hydrolase From Clostridium Perfringens also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of CBM32-1 From A Family 31 Glycoside Hydrolase From Clostridium Perfringens (pdb code 4lpl). 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 Structure of CBM32-1 From A Family 31 Glycoside Hydrolase From Clostridium Perfringens, PDB code: 4lpl:

Calcium binding site 1 out of 1 in 4lpl

Go back to Calcium Binding Sites List in 4lpl
Calcium binding site 1 out of 1 in the Structure of CBM32-1 From A Family 31 Glycoside Hydrolase From Clostridium Perfringens


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of CBM32-1 From A Family 31 Glycoside Hydrolase From Clostridium Perfringens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1101

b:11.2
occ:1.00
O A:LYS979 2.3 12.3 1.0
O A:ASP984 2.3 13.3 1.0
OE2 A:GLU1090 2.3 14.5 1.0
O A:ARG1089 2.4 10.1 1.0
O A:SER987 2.4 10.7 1.0
OD1 A:ASP982 2.4 12.8 1.0
OG A:SER987 2.5 13.1 1.0
C A:SER987 3.3 11.4 1.0
CD A:GLU1090 3.4 16.4 1.0
C A:ASP984 3.4 13.4 1.0
CG A:ASP982 3.5 14.8 1.0
C A:LYS979 3.5 12.3 1.0
C A:ARG1089 3.5 9.4 1.0
CB A:SER987 3.7 13.3 1.0
CG A:GLU1090 3.8 19.1 1.0
OD2 A:ASP982 3.8 15.7 1.0
CA A:SER987 3.9 13.0 1.0
N A:ASP984 4.0 14.2 1.0
N A:SER987 4.0 13.2 1.0
CA A:ASP984 4.1 15.0 1.0
CB A:ASP984 4.2 14.9 1.0
N A:GLN988 4.3 12.3 1.0
CA A:ARG1089 4.3 10.0 1.0
CA A:LYS979 4.4 13.1 1.0
N A:ALA980 4.4 10.9 1.0
N A:ASP982 4.5 14.2 1.0
CA A:ALA980 4.5 10.3 1.0
OE1 A:GLU1090 4.5 22.1 1.0
N A:ASP985 4.5 13.0 1.0
N A:GLU1090 4.5 9.5 1.0
C A:ALA980 4.6 11.1 1.0
CA A:GLN988 4.6 11.8 1.0
CB A:LYS979 4.6 14.8 1.0
CA A:GLU1090 4.7 9.8 1.0
CB A:ASP982 4.7 14.5 1.0
CA A:ASP985 4.8 13.4 1.0
N A:GLY983 4.8 14.2 1.0
CB A:GLU1090 4.8 11.6 1.0
C A:ASP985 4.8 12.7 1.0
N A:VAL981 4.8 10.2 1.0
CB A:ARG1089 4.9 10.4 1.0
O A:ALA980 4.9 11.0 1.0
CA A:ASP982 5.0 14.1 1.0

Reference:

J.M.Grondin, D.Duan, C.A.Spencer, J.S.Allingham, S.P.Smith. Carbohydrate Recognition From A Family 31 Glycoside Hydrolase From Clostridium Perfringens To Be Published.
Page generated: Sun Jul 14 09:43:18 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy