5LK5

Crystal structure of the globular domain of human calreticulin mutant D71K

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

site_id	SWS_FT_FI1
Number of Residues	110
Details	Repeat: {"description":"1-1"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	537
Details	Region: {"description":"N-domain"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21423620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27840680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3POS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3POW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LK5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	50
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P14211","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	20
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	10
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---