1Z5O

Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0008782	molecular_function	adenosylhomocysteine nucleosidase activity
A	0008930	molecular_function	methylthioadenosine nucleosidase activity
A	0009086	biological_process	methionine biosynthetic process
A	0009116	biological_process	nucleoside metabolic process
A	0009164	biological_process	nucleoside catabolic process
A	0016787	molecular_function	hydrolase activity
A	0019284	biological_process	L-methionine salvage from S-adenosylmethionine
A	0019509	biological_process	L-methionine salvage from methylthioadenosine
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046124	biological_process	purine deoxyribonucleoside catabolic process
A	0110052	biological_process	toxic metabolite repair
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0008782	molecular_function	adenosylhomocysteine nucleosidase activity
B	0008930	molecular_function	methylthioadenosine nucleosidase activity
B	0009086	biological_process	methionine biosynthetic process
B	0009116	biological_process	nucleoside metabolic process
B	0009164	biological_process	nucleoside catabolic process
B	0016787	molecular_function	hydrolase activity
B	0019284	biological_process	L-methionine salvage from S-adenosylmethionine
B	0019509	biological_process	L-methionine salvage from methylthioadenosine
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046124	biological_process	purine deoxyribonucleoside catabolic process
B	0110052	biological_process	toxic metabolite repair

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MTA A 5233

Chain	Residue
A	SER76
A	ARG193
A	ASN197
A	PHE207
A	HOH5234
A	HOH5277
A	ALA77
A	GLY78
A	ALA150
A	PHE151
A	ILE152
A	GLU172
A	MET173
A	GLU174

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTA B 9233

Chain	Residue
B	ALA8
B	ILE50
B	SER76
B	ALA77
B	GLY78
B	ALA150
B	PHE151
B	ILE152
B	GLU172
B	MET173
B	GLU174
B	ARG193
B	ASN197
B	PHE207
B	HOH9243
B	HOH9251

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16109423","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16109423","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11591349","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01684","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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