Atomistry » Calcium » PDB 1jf5-1jv2 » 1jfh
Atomistry »
  Calcium »
    PDB 1jf5-1jv2 »
      1jfh »

Calcium in PDB 1jfh: Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution

Enzymatic activity of Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution

All present enzymatic activity of Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution:
3.2.1.1;

Protein crystallography data

The structure of Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution, PDB code: 1jfh was solved by M.Qian, F.Payan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 2.03
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.300, 87.800, 103.400, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 18.5

Other elements in 1jfh:

The structure of Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution also contains other interesting chemical elements:

Mercury (Hg) 1 atom
Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution (pdb code 1jfh). 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 A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution, PDB code: 1jfh:

Calcium binding site 1 out of 1 in 1jfh

Go back to Calcium Binding Sites List in 1jfh
Calcium binding site 1 out of 1 in the Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca500

b:9.8
occ:1.00
 O A:HIS201 2.4 7.8 1.0
OD1 A:ASN100 2.4 8.5 1.0
O A:ARG158 2.4 9.8 1.0
OD2 A:ASP167 2.5 10.8 1.0
O A:HOH539 2.5 12.9 1.0
OD1 A:ASP167 2.6 14.2 1.0
O A:HOH527 2.6 7.2 1.0
O A:HOH520 2.6 10.8 1.0
CG A:ASP167 2.9 12.8 1.0
C A:ARG158 3.4 8.9 1.0
CG A:ASN100 3.4 9.3 1.0
C A:HIS201 3.6 9.0 1.0
ND2 A:ASN100 3.8 7.7 1.0
CA A:ARG158 4.1 10.8 1.0
CB A:HIS201 4.3 10.1 1.0
O A:ASN100 4.4 8.4 1.0
CB A:ASP167 4.4 9.3 1.0
N A:ASP159 4.5 9.3 1.0
CG A:MET202 4.5 11.3 1.0
CA A:HIS201 4.5 8.4 1.0
N A:MET202 4.5 9.8 1.0
O A:HOH556 4.5 15.9 1.0
ND2 A:ASN137 4.6 13.7 1.0
CA A:MET202 4.6 10.0 1.0
O A:CYS160 4.6 10.9 1.0
CA A:ASP159 4.7 9.5 1.0
CB A:ASN100 4.8 5.9 1.0
O A:VAL157 4.8 9.9 1.0
O A:LEU168 4.8 8.6 1.0
CB A:ARG158 4.8 12.5 1.0

Reference:

M.Qian, S.Spinelli, H.Driguez, F.Payan. Structure of A Pancreatic Alpha-Amylase Bound to A Substrate Analogue at 2.03 A Resolution. Protein Sci. V. 6 2285 1997.
ISSN: ISSN 0961-8368
PubMed: 9385631
Page generated: Thu Jul 11 10:45:12 2024

Last articles

Zn in 1MC5
Zn in 1MFM
Zn in 1MA0
Zn in 1MED
Zn in 1MEA
Zn in 1MBX
Zn in 1MA3
Zn in 1M9O
Zn in 1M9R
Zn in 1M9Q
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy