Structure of PDB 5j6d Chain A Binding Site BS02

Receptor Information
>5j6d Chain A (length=292) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
METVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADL
AMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLS
KYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFH
CTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGAS
EEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKV
KPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTI
Ligand information
Ligand ID6H5
InChIInChI=1S/C30H35N5O5/c1-39-22-7-5-8-23(18-22)40-27-10-6-9-26(35-15-3-2-4-16-35)24(27)19-33-30(32)34-28(36)21-13-11-20(12-14-21)17-25(31)29(37)38/h5-14,18,25H,2-4,15-17,19,31H2,1H3,(H,37,38)(H3,32,33,34,36)/t25-/m0/s1
InChIKeyUDMPHIGEFLMAIW-VWLOTQADSA-N
SMILES
SoftwareSMILES
CACTVS 3.385COc1cccc(Oc2cccc(N3CCCCC3)c2CNC(=N)NC(=O)c4ccc(C[CH](N)C(O)=O)cc4)c1
OpenEye OEToolkits 2.0.4COc1cccc(c1)Oc2cccc(c2CNC(=N)NC(=O)c3ccc(cc3)CC(C(=O)O)N)N4CCCCC4
OpenEye OEToolkits 2.0.4[H]/N=C(/NCc1c(cccc1Oc2cccc(c2)OC)N3CCCCC3)\NC(=O)c4ccc(cc4)C[C@@H](C(=O)O)N
CACTVS 3.385COc1cccc(Oc2cccc(N3CCCCC3)c2CNC(=N)NC(=O)c4ccc(C[C@H](N)C(O)=O)cc4)c1
ACDLabs 12.01N(\C(=N)NCc1c(cccc1Oc2cccc(c2)OC)N3CCCCC3)C(=O)c4ccc(cc4)CC(C(=O)O)N
FormulaC30 H35 N5 O5
Name4-[(N-{[2-(3-methoxyphenoxy)-6-(piperidin-1-yl)phenyl]methyl}carbamimidoyl)carbamoyl]-L-phenylalanine
ChEMBLCHEMBL3797264
DrugBank
ZINCZINC000584904855
PDB chain5j6d Chain A Residue 504 [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]
PDB5j6d Discovery of acyl guanidine tryptophan hydroxylase-1 inhibitors.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		L129 Y235 L236 R257 Y264 T265 P266 P268 H272 A309 Y312 F313 E317 S336 S337 I366
Binding residue
(residue number reindexed from 1)		L28 Y134 L135 R156 Y163 T164 P165 P167 H171 A208 Y211 F212 E216 S235 S236 I265
Annotation score1
Binding affinityMOAD: ic50=6nM
PDBbind-CN: -logKd/Ki=8.22,IC50=6nM
Enzymatic activity
Catalytic site (original residue number in PDB) H272 H277 E317 S336
Catalytic site (residue number reindexed from 1) H171 H176 E216 S235
Enzyme Commision number 1.14.16.4: tryptophan 5-monooxygenase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016714 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0009072 aromatic amino acid metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5j6d, PDBe:5j6d, PDBj:5j6d
PDBsum5j6d
PubMed27146606
UniProtP17752|TPH1_HUMAN Tryptophan 5-hydroxylase 1 (Gene Name=TPH1)

[Back to BioLiP]