Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0006457 | biological_process | protein folding |
A | 0051082 | molecular_function | unfolded protein binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0006457 | biological_process | protein folding |
B | 0051082 | molecular_function | unfolded protein binding |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005783 | cellular_component | endoplasmic reticulum |
C | 0006457 | biological_process | protein folding |
C | 0051082 | molecular_function | unfolded protein binding |
D | 0005509 | molecular_function | calcium ion binding |
D | 0005783 | cellular_component | endoplasmic reticulum |
D | 0006457 | biological_process | protein folding |
D | 0051082 | molecular_function | unfolded protein binding |
E | 0005509 | molecular_function | calcium ion binding |
E | 0005783 | cellular_component | endoplasmic reticulum |
E | 0006457 | biological_process | protein folding |
E | 0051082 | molecular_function | unfolded protein binding |
F | 0005509 | molecular_function | calcium ion binding |
F | 0005783 | cellular_component | endoplasmic reticulum |
F | 0006457 | biological_process | protein folding |
F | 0051082 | molecular_function | unfolded protein binding |
G | 0005509 | molecular_function | calcium ion binding |
G | 0005783 | cellular_component | endoplasmic reticulum |
G | 0006457 | biological_process | protein folding |
G | 0051082 | molecular_function | unfolded protein binding |
H | 0005509 | molecular_function | calcium ion binding |
H | 0005783 | cellular_component | endoplasmic reticulum |
H | 0006457 | biological_process | protein folding |
H | 0051082 | molecular_function | unfolded protein binding |
I | 0005509 | molecular_function | calcium ion binding |
I | 0005783 | cellular_component | endoplasmic reticulum |
I | 0006457 | biological_process | protein folding |
I | 0051082 | molecular_function | unfolded protein binding |
J | 0005509 | molecular_function | calcium ion binding |
J | 0005783 | cellular_component | endoplasmic reticulum |
J | 0006457 | biological_process | protein folding |
J | 0051082 | molecular_function | unfolded protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 500 |
Chain | Residue |
A | GLN26 |
A | LYS62 |
A | LYS64 |
A | ASP328 |
A | HOH618 |
A | HOH636 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA B 500 |
Chain | Residue |
B | ASP328 |
B | HOH609 |
B | HOH629 |
B | GLN26 |
B | LYS62 |
B | LYS64 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA C 500 |
Chain | Residue |
C | GLN26 |
C | LYS62 |
C | LYS64 |
C | ASP328 |
C | HOH621 |
C | HOH630 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA D 500 |
Chain | Residue |
D | GLN26 |
D | LYS62 |
D | LYS64 |
D | ASP328 |
D | HOH636 |
D | HOH647 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CA E 401 |
Chain | Residue |
E | GLN26 |
E | LYS62 |
E | LYS64 |
E | ASP328 |
E | HOH529 |
E | HOH533 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue CL E 402 |
Chain | Residue |
D | GLY205 |
D | SER206 |
E | LEU51 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CA F 500 |
Chain | Residue |
F | GLN26 |
F | LYS62 |
F | LYS64 |
F | ASP328 |
F | HOH634 |
F | HOH648 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA G 401 |
Chain | Residue |
G | GLN26 |
G | LYS62 |
G | LYS64 |
G | ASP328 |
G | HOH518 |
G | HOH524 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue CA H 500 |
Chain | Residue |
H | GLN26 |
H | LYS62 |
H | LYS64 |
H | ASP328 |
H | HOH628 |
H | HOH630 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue CA I 500 |
Chain | Residue |
I | GLN26 |
I | LYS62 |
I | LYS64 |
I | ASP328 |
I | HOH634 |
I | HOH637 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue CA J 500 |
Chain | Residue |
J | GLN26 |
J | LYS62 |
J | LYS64 |
J | ASP328 |
J | HOH636 |
J | HOH639 |
Functional Information from PROSITE/UniProt
site_id | PS00803 |
Number of Residues | 16 |
Details | CALRETICULIN_1 Calreticulin family signature 1. KhEQnidCGGGYVKLF |
Chain | Residue | Details |
A | LYS98-PHE113 | |
site_id | PS00804 |
Number of Residues | 9 |
Details | CALRETICULIN_2 Calreticulin family signature 2. IMFGPDiCG |
Chain | Residue | Details |
A | ILE130-GLY138 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLN26 | |
C | LYS62 | |
C | LYS64 | |
C | ASP328 | |
D | GLN26 | |
D | LYS62 | |
D | LYS64 | |
D | ASP328 | |
E | GLN26 | |
E | LYS62 | |
E | LYS64 | |
A | LYS62 | |
E | ASP328 | |
F | GLN26 | |
F | LYS62 | |
F | LYS64 | |
F | ASP328 | |
G | GLN26 | |
G | LYS62 | |
G | LYS64 | |
G | ASP328 | |
H | GLN26 | |
A | LYS64 | |
H | LYS62 | |
H | LYS64 | |
H | ASP328 | |
I | GLN26 | |
I | LYS62 | |
I | LYS64 | |
I | ASP328 | |
J | GLN26 | |
J | LYS62 | |
J | LYS64 | |
A | ASP328 | |
J | ASP328 | |
B | GLN26 | |
B | LYS62 | |
B | LYS64 | |
B | ASP328 | |
C | GLN26 | |
Chain | Residue | Details |
A | TYR109 | |
B | ASP317 | |
C | TYR109 | |
C | LYS111 | |
C | TYR128 | |
C | ASP135 | |
C | ASP317 | |
D | TYR109 | |
D | LYS111 | |
D | TYR128 | |
D | ASP135 | |
A | LYS111 | |
D | ASP317 | |
E | TYR109 | |
E | LYS111 | |
E | TYR128 | |
E | ASP135 | |
E | ASP317 | |
F | TYR109 | |
F | LYS111 | |
F | TYR128 | |
F | ASP135 | |
A | TYR128 | |
F | ASP317 | |
G | TYR109 | |
G | LYS111 | |
G | TYR128 | |
G | ASP135 | |
G | ASP317 | |
H | TYR109 | |
H | LYS111 | |
H | TYR128 | |
H | ASP135 | |
A | ASP135 | |
H | ASP317 | |
I | TYR109 | |
I | LYS111 | |
I | TYR128 | |
I | ASP135 | |
I | ASP317 | |
J | TYR109 | |
J | LYS111 | |
J | TYR128 | |
J | ASP135 | |
A | ASP317 | |
J | ASP317 | |
B | TYR109 | |
B | LYS111 | |
B | TYR128 | |
B | ASP135 | |
Chain | Residue | Details |
A | LYS48 | |
E | LYS159 | |
F | LYS48 | |
F | LYS159 | |
G | LYS48 | |
G | LYS159 | |
H | LYS48 | |
H | LYS159 | |
I | LYS48 | |
I | LYS159 | |
J | LYS48 | |
A | LYS159 | |
J | LYS159 | |
B | LYS48 | |
B | LYS159 | |
C | LYS48 | |
C | LYS159 | |
D | LYS48 | |
D | LYS159 | |
E | LYS48 | |
Chain | Residue | Details |
A | LYS64 | |
J | LYS64 | |
B | LYS64 | |
C | LYS64 | |
D | LYS64 | |
E | LYS64 | |
F | LYS64 | |
G | LYS64 | |
H | LYS64 | |
I | LYS64 | |
Chain | Residue | Details |
A | ASN344 | |
J | ASN344 | |
B | ASN344 | |
C | ASN344 | |
D | ASN344 | |
E | ASN344 | |
F | ASN344 | |
G | ASN344 | |
H | ASN344 | |
I | ASN344 | |