6AYQ

Crystal structure of Campylobacter jejuni 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with methylthio-DADMe-Immucillin-A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
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	0009234	biological_process	menaquinone biosynthetic 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	0102246	molecular_function	6-amino-6-deoxyfutalosine hydrolase activity
B	0003824	molecular_function	catalytic activity
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	0009234	biological_process	menaquinone biosynthetic 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	0102246	molecular_function	6-amino-6-deoxyfutalosine hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue TDI A 301

Chain	Residue
A	ALA8
A	GLU171
A	MET172
A	GLU173
A	SER195
A	ASP196
A	PHE206
A	HOH420
B	ILE102
B	PHE105
A	ILE50
A	VAL76
A	ALA77
A	GLY78
A	GLU150
A	PHE151
A	ILE152
A	CYS170

---

site_id	AC2
Number of Residues	18
Details	binding site for residue TDI B 301

Chain	Residue
A	ILE102
A	PHE105
B	ALA8
B	ILE50
B	VAL76
B	ALA77
B	GLY78
B	GLU150
B	PHE151
B	ILE152
B	CYS170
B	GLU171
B	MET172
B	GLU173
B	SER195
B	ASP196
B	PHE206
B	HOH417

---

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL B 302

Chain	Residue
A	GLU116
A	ASP207
B	PHE105
B	HIS107
B	PRO113
B	HOH410

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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