Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

I-TASSER I-TASSER-MTD C-I-TASSER CR-I-TASSER QUARK C-QUARK LOMETS MUSTER CEthreader SEGMER DeepFold DeepFoldRNA FoldDesign COFACTOR COACH MetaGO TripletGO IonCom FG-MD ModRefiner REMO DEMO DEMO-EM SPRING COTH Threpp PEPPI BSpred ANGLOR EDock BSP-SLIM SAXSTER FUpred ThreaDom ThreaDomEx EvoDesign BindProf BindProfX SSIPe GPCR-I-TASSER MAGELLAN ResQ STRUM DAMpred

TM-score TM-align US-align MM-align RNA-align NW-align LS-align EDTSurf MVP MVP-Fit SPICKER HAAD PSSpred 3DRobot MR-REX I-TASSER-MR SVMSEQ NeBcon ResPRE TripletRes DeepPotential WDL-RF ATPbind DockRMSD DeepMSA FASPR EM-Refiner GPU-I-TASSER

BioLiP E. coli GLASS GPCR-HGmod GPCR-RD GPCR-EXP Tara-3D TM-fold DECOYS POTENTIAL RW/RWplus EvoEF HPSF THE-DB ADDRESS Alpaca-Antibody CASP7 CASP8 CASP9 CASP10 CASP11 CASP12 CASP13 CASP14

BioLiP

Structure of PDB 2vou Chain C Binding Site BS02

Receptor Information
>2vou Chain C (length=387) Species: 29320 (Paenarthrobacter nicotinovorans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SPTTDRIAVVGGSISGLTAALMLRDAGVDVDVYERSPQPLSGFGTGIVVQ
PELVHYLLEQGVELDSISVPSSSMEYVDALTGERVGSVPADWRFTSYDSI
YGGLYELFGPERYHTSKCLVGLSQDSETVQMRFSDGTKAEANWVIGADGG
ASVVRKRLLGIEPTYAGYVTWRGVLQPGEVADDVWNYFNDKFTYGLLDDG
HLIAYPIPGRENAESPRLNFQWYWNVAEGPDLDELMTDVRGIRLPTSVHN
NSLNPHNLRQFHSKGESLFKPFRDLVLNASSPFVTVVADATVDRMVHGRV
LLIGDAAVTPRPHAAAGGAKASDDARTLAEVFTKNHDLRGSLQSWETRQL
QQGHAYLNKVKKMASRLQHGGSFEPGNPAFAFGLPKV
Ligand information
Ligand IDGOL
InChIInChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
InChIKeyPEDCQBHIVMGVHV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C(C(CO)O)O
ACDLabs 12.01
CACTVS 3.370
OCC(O)CO
FormulaC3 H8 O3
NameGLYCEROL;
GLYCERIN;
PROPANE-1,2,3-TRIOL
ChEMBLCHEMBL692
DrugBankDB09462
ZINCZINC000000895048
PDB chain2vou Chain C Residue 1390 [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]
PDB2vou Structure of 2,6-Dihydroxypyridine 3-Hydroxylase from a Nicotine-Degrading Pathway.
Resolution2.6 Å
Binding residue
(original residue number in PDB)
Y206 Q222 Y224 P313
Binding residue
(residue number reindexed from 1)
Y205 Q221 Y223 P312
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.13.10: 2,6-dihydroxypyridine 3-monooxygenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0018663 2,6-dihydroxypyridine 3-monooxygenase activity
GO:0042803 protein homodimerization activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0019608 nicotine catabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:2vou, PDBe:2vou, PDBj:2vou
PDBsum2vou
PubMed18440023
UniProtQ93NG3|DHPH_PAENI 2,6-dihydroxypyridine 3-monooxygenase (Gene Name=dhpH)

[Back to BioLiP]

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417