Structure of PDB 6i3d Chain B Binding Site BS03

Receptor Information
>6i3d Chain B (length=218) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NLYFQGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKK
GKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCA
AITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDR
YLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQS
FLEYREVVDGLEKAIYKG
Ligand information
Ligand IDSFG
InChIInChI=1S/C15H23N7O5/c16-6(1-2-7(17)15(25)26)3-8-10(23)11(24)14(27-8)22-5-21-9-12(18)19-4-20-13(9)22/h4-8,10-11,14,23-24H,1-3,16-17H2,(H,25,26)(H2,18,19,20)/t6-,7-,8+,10+,11+,14+/m0/s1
InChIKeyLMXOHSDXUQEUSF-YECHIGJVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)C[C@H](CC[C@@H](C(=O)O)N)N)O)O)N
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CC(CCC(C(=O)O)N)N)O)O)N
CACTVS 3.370N[CH](CC[CH](N)C(O)=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
CACTVS 3.370N[C@@H](CC[C@H](N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
ACDLabs 12.01O=C(O)C(N)CCC(N)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H23 N7 O5
NameSINEFUNGIN;
ADENOSYL-ORNITHINE
ChEMBLCHEMBL1214186
DrugBankDB01910
ZINCZINC000004217451
PDB chain6i3d Chain B Residue 303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6i3d Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-O-methyltransferase.
Resolution1.45 Å
Binding residue
(original residue number in PDB)		M40 N41 V42 G66 Y68 Y71 S72 E90 I91 S119 D141 H142 W143
Binding residue
(residue number reindexed from 1)		M44 N45 V46 G70 Y72 Y75 S76 E94 I95 S123 D145 H146 W147
Annotation score3
Enzymatic activity
Enzyme Commision number 2.1.1.6: catechol O-methyltransferase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008171 O-methyltransferase activity
GO:0016206 catechol O-methyltransferase activity
Biological Process
GO:0006584 catecholamine metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6i3d, PDBe:6i3d, PDBj:6i3d
PDBsum6i3d
PubMed31080692
UniProtP21964|COMT_HUMAN Catechol O-methyltransferase (Gene Name=COMT)

[Back to BioLiP]