1NUR

CRYSTAL STRUCTURE OF HUMAN CYTOSOLIC NMN/NaMN ADENYLYLTRANSFERASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000309	molecular_function	nicotinamide-nucleotide adenylyltransferase activity
A	0003824	molecular_function	catalytic activity
A	0004515	molecular_function	nicotinate-nucleotide adenylyltransferase activity
A	0005524	molecular_function	ATP binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0009058	biological_process	biosynthetic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0009435	biological_process	NAD biosynthetic process
A	0009611	biological_process	response to wounding
A	0016779	molecular_function	nucleotidyltransferase activity
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0030424	cellular_component	axon
A	0034612	biological_process	response to tumor necrosis factor
A	0043025	cellular_component	neuronal cell body
A	0070566	molecular_function	adenylyltransferase activity
B	0000309	molecular_function	nicotinamide-nucleotide adenylyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0004515	molecular_function	nicotinate-nucleotide adenylyltransferase activity
B	0005524	molecular_function	ATP binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0009058	biological_process	biosynthetic process
B	0009165	biological_process	nucleotide biosynthetic process
B	0009435	biological_process	NAD biosynthetic process
B	0009611	biological_process	response to wounding
B	0016779	molecular_function	nucleotidyltransferase activity
B	0019363	biological_process	pyridine nucleotide biosynthetic process
B	0030424	cellular_component	axon
B	0034612	biological_process	response to tumor necrosis factor
B	0043025	cellular_component	neuronal cell body
B	0070566	molecular_function	adenylyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	LYS95
A	ARG98
A	HIS152
A	HOH493

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 302

Chain	Residue
A	HOH415
A	HOH480
A	HOH481
A	HOH634
A	HOH639
A	SER14
A	LYS56
A	ALA202
A	THR203
A	ARG206

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 303

Chain	Residue
B	ARG98
B	HIS152

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site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 304

Chain	Residue
A	HOH544
B	SER14
B	ALA202
B	THR203
B	ARG206
B	HOH438
B	HOH440
B	HOH520
B	HOH640

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 305

Chain	Residue
A	LYS173
B	LYS193
B	PRO195
B	ARG207

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:12574164, ECO:0007744|PDB:1NUU

Chain	Residue	Details
A	SER14
A	ASN198
B	SER14
B	PHE15
B	TRP90
B	THR93
B	GLY135
B	ASP137
B	LEU147
B	TRP148
B	ARG167
A	PHE15
B	ASN198
A	TRP90
A	THR93
A	GLY135
A	ASP137
A	LEU147
A	TRP148
A	ARG167

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: in other chain => ECO:0000269|PubMed:12574164

Chain	Residue	Details
A	HIS22
A	LYS56
A	THR203
B	HIS22
B	LYS56
B	THR203

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:12574164

Chain	Residue	Details
A	LYS140
B	LYS140

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