1JYS

Crystal Structure of E. coli MTA/AdoHcy Nucleosidase

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	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	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	8
Details	BINDING SITE FOR RESIDUE ADE A 233

Chain	Residue
A	GLY78
A	ALA150
A	PHE151
A	ILE152
A	GLU172
A	MET173
A	HOH234
A	HOH320

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site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ADE B 234

Chain	Residue
B	ALA150
B	PHE151
B	ILE152
B	GLU172
B	MET173
B	HOH322
B	HOH323
B	GLY78

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:16109423

Chain	Residue	Details
A	GLU12
B	GLU12

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:16109423

Chain	Residue	Details
A	ASP197
B	ASP197

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000269|PubMed:11591349

Chain	Residue	Details
A	GLY78
A	ILE152
B	GLY78
B	ILE152

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01684

Chain	Residue	Details
A	MET173
B	MET173

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
A	ASP197
A	PHE210

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a69

Chain	Residue	Details
B	ASP197
B	PHE210

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