Structure of PDB 4wxh Chain A Binding Site BS02

Receptor Information

>4wxh Chain A (length=344) Species: 1950 (Streptomyces peucetius)

RPQQIDALRTLIRLGSLHTPMVVRTAATLRLVDHILAGARTVKALAARTD
TRPEALLRLIRHLVAIGLLEEDAPGEFVPTEVGELLADDHPAAQRAWHDL
TQAVARADISFTRLPDAIRTGRPTYESIYGKPFYEDLAGRPDLRASFDSL
LACDQDVAFDAPAAAYDWTNVRHVLDVGGGKGGFAAAIARRAPHVSATVL
EMAGTVDTARSYLKDEGLSDRVDVVEGDFFEPLPRKADAIILSFVLLNWP
DHDAVRILTRCAEALEPGGRILIHERDDLHENSFNEQFSTELDLRMLVFL
GGALRTREKWDGLAASAGLVVEEVRQLPSPTIPYDLSLLVLAPA

Ligand information

• Ligand ID: 3VL
• InChI: InChI=1S/C30H35NO10/c1-6-30(38)12-19(41-20-11-17(31(3)4)25(33)13(2)40-20)22-15(24(30)29(37)39-5)10-16-23(28(22)36)27(35)21-14(26(16)34)8-7-9-18(21)32/h7-10,13,17,19-20,24-25,32-33,36,38H,6,11-12H2,1-5H3/t13-,17-,19-,20-,24-,25+,30+/m0/s1
• InChIKey: LJZPVWKMAYDYAS-QKKPTTNWSA-N
• SMILES:
  CACTVS 3.385: CC[C]1(O)C[CH](O[CH]2C[CH]([CH](O)[CH](C)O2)N(C)C)c3c(O)c4C(=O)c5c(O)cccc5C(=O)c4cc3[CH]1C(=O)OC
  OpenEye OEToolkits 1.7.6: CCC1(CC(c2c(cc3c(c2O)C(=O)c4c(cccc4O)C3=O)C1C(=O)OC)OC5CC(C(C(O5)C)O)N(C)C)O
  OpenEye OEToolkits 1.7.6: CC[C@]1(C[C@@H](c2c(cc3c(c2O)C(=O)c4c(cccc4O)C3=O)[C@H]1C(=O)OC)O[C@H]5C[C@@H]([C@@H]([C@@H](O5)C)O)N(C)C)O
  CACTVS 3.385: CC[C@@]1(O)C[C@H](O[C@H]2C[C@@H]([C@H](O)[C@H](C)O2)N(C)C)c3c(O)c4C(=O)c5c(O)cccc5C(=O)c4cc3[C@H]1C(=O)OC
  ACDLabs 12.01: O=C(OC)C5c3cc2C(=O)c1cccc(O)c1C(=O)c2c(O)c3C(OC4OC(C(O)C(N(C)C)C4)C)CC5(O)CC
• Formula: C30 H35 N O10
• Name: methyl (1R,2R,4S)-2-ethyl-2,5,7-trihydroxy-6,11-dioxo-4-{[2,3,6-trideoxy-3-(dimethylamino)-alpha-L-lyxo-hexopyranosyl]oxy}-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate;
  aclacinomycin T
• ChEMBL: CHEMBL3040622
• ZINC: ZINC000003977735
• PDB chain: 4wxh Chain A Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4wxh Divergent evolution of an atypical S-adenosyl-l-methionine-dependent monooxygenase involved in anthracycline biosynthesis.
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): W105 F155 L159 D162 F252 E299 L300 R303 M304 F307
• Binding residue (residue number reindexed from 1): W97 F147 L151 D154 F244 E291 L292 R295 M296 F299
• Annotation score: 2

Enzymatic activity

• Catalytic site (original residue number in PDB): L255 N256 E283 L312
• Catalytic site (residue number reindexed from 1): L247 N248 E275 L304
• Enzyme Commision number: 2.1.1.292: carminomycin 4-O-methyltransferase.

Gene Ontology

Molecular Function

• GO:0008168 methyltransferase activity
• GO:0008171 O-methyltransferase activity

External links

• PDB: RCSB:4wxh, PDBe:4wxh, PDBj:4wxh
• PDBsum: 4wxh
• PubMed: 26216966
• UniProt: Q06528|DNRK_STRPE Carminomycin 4-O-methyltransferase DnrK (Gene Name=dnrK)