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Calcium in PDB 1vah: Crystal Structure of the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside

Enzymatic activity of Crystal Structure of the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside

All present enzymatic activity of Crystal Structure of the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside:
3.2.1.1;

Protein crystallography data

The structure of Crystal Structure of the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside, PDB code: 1vah was solved by H.Zhuo, F.Payan, M.Qian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 2.40
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 (%) 17 / 23.3

Other elements in 1vah:

The structure of Crystal Structure of the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside (pdb code 1vah). 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 Crystal Structure of the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside, PDB code: 1vah:

Calcium binding site 1 out of 1 in 1vah

Go back to Calcium Binding Sites List in 1vah
Calcium binding site 1 out of 1 in the Crystal Structure of the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside


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 the Pig Pancreatic-Amylase Complexed with R- Nitrophenyl-A-D-Maltoside within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca500

b:11.6
occ:1.00
 O A:ARG158 2.3 12.6 1.0
OD2 A:ASP167 2.3 7.9 1.0
OD1 A:ASN100 2.4 6.9 1.0
O A:HIS201 2.5 6.0 1.0
OD1 A:ASP167 2.5 8.9 1.0
CG A:ASP167 2.8 9.5 1.0
C A:ARG158 3.3 12.7 1.0
CG A:ASN100 3.5 7.3 1.0
C A:HIS201 3.7 8.7 1.0
CA A:ARG158 3.9 11.5 1.0
ND2 A:ASN100 4.0 3.2 1.0
N A:ASP159 4.2 14.5 1.0
CB A:ASP167 4.3 10.0 1.0
CB A:HIS201 4.4 10.6 1.0
O A:HOH536 4.4 9.9 1.0
ND2 A:ASN137 4.5 11.8 1.0
O A:CYS160 4.5 15.2 1.0
O A:ASN100 4.5 11.1 1.0
O A:VAL157 4.5 13.0 1.0
CA A:ASP159 4.5 12.9 1.0
CA A:HIS201 4.6 9.9 1.0
N A:MET202 4.6 8.0 1.0
CG A:MET202 4.6 9.8 1.0
CA A:MET202 4.7 9.1 1.0
CB A:ASN100 4.8 4.9 1.0
CB A:ARG158 4.9 10.4 1.0
C A:ASP159 4.9 13.7 1.0
O A:LEU168 4.9 11.9 1.0
O A:HOH528 5.0 7.1 1.0

Reference:

H.Zhuo, F.Payan, M.Qian. Crystal Structure of the Pig Pancreatic Alpha-Amylase Complexed with Rho-Nitrophenyl-Alpha-D-Maltoside-Flexibility in the Active Site Protein J. V. 23 379 2004.
ISSN: ISSN 1572-3887
PubMed: 15517985
DOI: 10.1023/B:JOPC.0000039552.94529.95
Page generated: Fri Jul 12 00:01:35 2024

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