Structure of PDB 3i5u Chain A

Receptor sequence
>3i5uA (length=325) Species: 167636 (Streptomyces carzinostaticus subsp. neocarzinostaticus) [Search protein sequence]
AAHIGLRALADLATPMAVRVAATLRVADHIAAGHRTAAEIASAAGAHADS
LDRLLRHLVAVGLFTRDGQGVYGLTEFGEQLRDDHAAGKRKWLDMNSAVG
RGDLGFVELAHSIRTGQPAYPVRYGTSFWEDLGSDPVLSASFDTLMSHHL
ELDYTGIAAKYDWAALGHVVDVGGGSGGLLSALLTAHEDLSGTVLDLQGP
ASAAHRRFLDTGLSGRAQVVVGSFFDPLPAGAGGYVLSAVLHDWDDLSAV
AILRRCAEAAGSGGVVLVIEAVAGAGTGMDLRMLTYFGGKERSLAELGEL
AAQAGLAVRAAHPISYVSIVEMTAL
3D structure
PDB3i5u Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H246 D247 E274 E298
Catalytic site (residue number reindexed from 1) H242 D243 E270 E291
Enzyme Commision number 2.1.1.303: 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase.
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 SAM A W133 F146 M150 G177 D200 L201 S227 F228 S242 A243 D247 W129 F142 M146 G173 D196 L197 S223 F224 S238 A239 D243
BS02 5NA A W96 F146 M150 M286 R289 Y293 W92 F142 M146 M279 R282 Y286
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3i5u, PDBe:3i5u, PDBj:3i5u
PDBsum3i5u
PubMed19702337
UniProtQ84HC8|NCSB1_STRCZ 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase (Gene Name=ncsB1)

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