Structure of PDB 1k4m Chain C

Receptor sequence
>1k4mC (length=213) Species: 562 (Escherichia coli) [Search protein sequence]
MKSLQALFGGTFDPVHYGHLKPVETLANLIGLTRVTIIPNNVPPHRPQPE
ANSVQRKHMLELAIADKPLFTLDERELKRNAPSYTAQTLKEWRQEQGPDV
PLAFIIGQDSLLTFPTWYEYETILDNAHLIVCRRPGYPLEMAQPQYQQWL
EDHLTHNPEDLHLQPAGKIYLAETPWFNISATIIRERLQNGESCEDLLPE
PVLTYINQQGLYR
3D structure
PDB1k4m Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD.
ChainC
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.18: nicotinate-nucleotide adenylyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD C F8 G9 G10 T11 G18 H19 N40 H45 R46 Y84 T85 I106 G107 D109 S110 W117 Y118 R134 F8 G9 G10 T11 G18 H19 N40 H45 R46 Y84 T85 I106 G107 D109 S110 W117 Y118 R134
Gene Ontology
Molecular Function
GO:0000309 nicotinamide-nucleotide adenylyltransferase activity
GO:0003824 catalytic activity
GO:0004515 nicotinate-nucleotide adenylyltransferase activity
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0070566 adenylyltransferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0034355 NAD salvage
GO:0034628 'de novo' NAD biosynthetic process from aspartate

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Molecular Function
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Biological Process
External links
PDB RCSB:1k4m, PDBe:1k4m, PDBj:1k4m
PDBsum1k4m
PubMed11796112
UniProtP0A752|NADD_ECOLI Nicotinate-nucleotide adenylyltransferase (Gene Name=nadD)

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