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●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

Structure of PDB 1w1t Chain A Binding Site BS02

Receptor Information >1w1t Chain A (length=496) Species: 615 (Serratia marcescens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] TRKAVIGYYFIPTNQINNYTETDTSVVPFPVSNITPAKAKQLTHINFSFL DINSNLECAWDPATNDAKARDVVNRLTALKAHNPSLRIMFSIGGWYYSND LGVSHANYVNAVKTPASRAKFAQSCVRIMKDYGFDGVDIDWEYPQAAEVD GFIAALQEIRTLLNQQTITDGRQALPYQLTIAGAGGAFFLSRYYSKLAQI VAPLDYINLMTYDLAGPWEKVTNHQAALFGDAAGPTFYNALREANLGWSW EELTRAFPSPFSLTVDAAVQQHLMMEGVPSAKIVMGVPFYGRAFKGVSGG NGGQYSSHSTPGEDPYPSTDYWLVGCEECVRDKDPRIASYRQLEQMLQGN YGYQRLWNDKTKTPYLYHAQNGLFVTYDDAESFKYKAKYIKQQQLGGVMF WHLGQDNRNGDLLAALDRYFNAADYDDSQLDMGTGLRYTGVGPGNLPIMT APAYVPGTTYAQGALVSYQGYVWQTKWGYITSAPGSDSAWLKVGRV

Ligand information Ligand ID CHQ InChI InChI=1S/C11H14N4O2/c16-10-9-2-1-3-15(9)11(17)8(14-10)4-7-5-12-6-13-7/h5-6,8-9H,1-4H2,(H,12,13)(H,14,16)/t8-,9-/m0/s1 InChIKey NAKUGCPAQTUSBE-IUCAKERBSA-N SMILES Software SMILES CACTVS 3.341 O=C1N[CH](Cc2[nH]cnc2)C(=O)N3CCC[CH]13 OpenEye OEToolkits 1.5.0 c1c([nH]cn1)C[C@H]2C(=O)N3CCC[C@H]3C(=O)N2 CACTVS 3.341 O=C1N[C@@H](Cc2[nH]cnc2)C(=O)N3CCC[C@@H]13 ACDLabs 10.04 O=C1N3CCCC3C(=O)NC1Cc2cncn2 OpenEye OEToolkits 1.5.0 c1c([nH]cn1)CC2C(=O)N3CCCC3C(=O)N2 Formula C11 H14 N4 O2 Name CYCLO-(L-HISTIDINE-L-PROLINE) INHIBITOR; (3S,8AR)-3-(1H-IMIDAZOL-5-YLMETHYL)HEXAHYDROPYRROLO[1,2-A]PYRAZINE-1,4-DIONE ChEMBL CHEMBL188225 DrugBank DB02414 ZINC ZINC000004899569 PDB chain 1w1t Chain A Residue 1514 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure 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] PDB 1w1t Structure-Based Exploration of Cyclic Dipeptide Chitinase Inhibitors Resolution 1.9 Å Binding residue (original residue number in PDB) W97 W220 Binding residue (residue number reindexed from 1) W95 W218 Annotation score 1 Binding affinity MOAD: ic50=1.1mM PDBbind-CN: -logKd/Ki=2.96,IC50=1.1mM

Enzymatic activity Catalytic site (original residue number in PDB) D140 D142 E144 Y214 Catalytic site (residue number reindexed from 1) D138 D140 E142 Y212 Enzyme Commision number 3.2.1.14: chitinase.

Gene Ontology Molecular Function GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds GO:0004568 chitinase activity GO:0008061 chitin binding GO:0016798 hydrolase activity, acting on glycosyl bonds GO:0030246 carbohydrate binding

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0006032	chitin catabolic process

	Cellular Component
GO:0005576	extracellular region

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