2O1T

Structure of Middle plus C-terminal domains (M+C) of GRP94

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0005524	molecular_function	ATP binding
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone
E	0005524	molecular_function	ATP binding
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
F	0005524	molecular_function	ATP binding
F	0006457	biological_process	protein folding
F	0016887	molecular_function	ATP hydrolysis activity
F	0051082	molecular_function	unfolded protein binding
F	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0005524	molecular_function	ATP binding
G	0006457	biological_process	protein folding
G	0016887	molecular_function	ATP hydrolysis activity
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone
H	0005524	molecular_function	ATP binding
H	0006457	biological_process	protein folding
H	0016887	molecular_function	ATP hydrolysis activity
H	0051082	molecular_function	unfolded protein binding
H	0140662	molecular_function	ATP-dependent protein folding chaperone
I	0005524	molecular_function	ATP binding
I	0006457	biological_process	protein folding
I	0016887	molecular_function	ATP hydrolysis activity
I	0051082	molecular_function	unfolded protein binding
I	0140662	molecular_function	ATP-dependent protein folding chaperone
J	0005524	molecular_function	ATP binding
J	0006457	biological_process	protein folding
J	0016887	molecular_function	ATP hydrolysis activity
J	0051082	molecular_function	unfolded protein binding
J	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Site: {"description":"Important for ATP hydrolysis","evidences":[{"source":"PubMed","id":"17936703","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14625","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P08113","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P08113","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	30
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---