9QYJ

Crystal structure of human S-adenosyl-L-homocysteine hydrolase in complex with adenosine and cadmium ions.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004013	molecular_function	adenosylhomocysteinase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0033353	biological_process	L-methionine cycle
A	0042470	cellular_component	melanosome
A	0070062	cellular_component	extracellular exosome
B	0004013	molecular_function	adenosylhomocysteinase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005829	cellular_component	cytosol
B	0033353	biological_process	L-methionine cycle
B	0042470	cellular_component	melanosome
B	0070062	cellular_component	extracellular exosome
C	0004013	molecular_function	adenosylhomocysteinase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005829	cellular_component	cytosol
C	0033353	biological_process	L-methionine cycle
C	0042470	cellular_component	melanosome
C	0070062	cellular_component	extracellular exosome
D	0004013	molecular_function	adenosylhomocysteinase activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0005829	cellular_component	cytosol
D	0033353	biological_process	L-methionine cycle
D	0042470	cellular_component	melanosome
D	0070062	cellular_component	extracellular exosome
E	0004013	molecular_function	adenosylhomocysteinase activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005783	cellular_component	endoplasmic reticulum
E	0005829	cellular_component	cytosol
E	0033353	biological_process	L-methionine cycle
E	0042470	cellular_component	melanosome
E	0070062	cellular_component	extracellular exosome
F	0004013	molecular_function	adenosylhomocysteinase activity
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005783	cellular_component	endoplasmic reticulum
F	0005829	cellular_component	cytosol
F	0033353	biological_process	L-methionine cycle
F	0042470	cellular_component	melanosome
F	0070062	cellular_component	extracellular exosome
G	0004013	molecular_function	adenosylhomocysteinase activity
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005783	cellular_component	endoplasmic reticulum
G	0005829	cellular_component	cytosol
G	0033353	biological_process	L-methionine cycle
G	0042470	cellular_component	melanosome
G	0070062	cellular_component	extracellular exosome
H	0004013	molecular_function	adenosylhomocysteinase activity
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005783	cellular_component	endoplasmic reticulum
H	0005829	cellular_component	cytosol
H	0033353	biological_process	L-methionine cycle
H	0042470	cellular_component	melanosome
H	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

site_id	PS00738
Number of Residues	15
Details	ADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQNhAAAAI

Chain	Residue	Details
A	SER78-ILE92

---

site_id	PS00739
Number of Residues	17
Details	ADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvavVaGYGdVGKGc.A

Chain	Residue	Details
A	GLY213-ALA229

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P10760","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	104
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12590576","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586999","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P50247","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---