Structure of PDB 3i53 Chain A

Receptor sequence
>3i53A (length=325) Species: 167636 (Streptomyces carzinostaticus subsp. neocarzinostaticus) [Search protein sequence]
AAHIGLRALADLATPMAVRVAATLRVADHIAAGHRTAAEIASAAGAHADS
LDRLLRHLVAVGLFTRDGQGVYGLTEFGEQLRDDHAAGKRKWLDMNSAVG
RGDLGFVELAHSIRTGQPAYPVRYGTSFWEDLGSDPVLSASFDTLMSHHL
ELDYTGIAAKYDWAALGHVVDVGGGSGGLLSALLTAHEDLSGTVLDLQGP
ASAAHRRFLDTGLSGRAQVVVGSFFDPLPAGAGGYVLSAVLHDWDDLSAV
AILRRCAEAAGSGGVVLVIEAVAGAGTGMDLRMLTYFGGKERSLAELGEL
AAQAGLAVRAAHPISYVSIVEMTAL
3D structure
PDB3i53 Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
ChainA
Resolution2.08 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 SAH A W133 F146 H153 G177 D200 L201 S227 F228 S242 W129 F142 H149 G173 D196 L197 S223 F224 S238
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:3i53, PDBe:3i53, PDBj:3i53
PDBsum3i53
PubMed19702337
UniProtQ84HC8|NCSB1_STRCZ 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase (Gene Name=ncsB1)

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