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Structure of PDB 5hvo Chain B Binding Site BS01

Receptor Information >5hvo Chain B (length=454) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] RLLIVSNRLPITIRYEFSMSGLSGLSKTTTFQWYGWPGLEVPEDELGSVK KRLKDEFNATPVFMDDKLADRHYNGFSNSILWPLLHYHPGEIVFDEGAWD AYREANLLFAKTIVKEAQDGDLIWVQDYHLMLLPELLRAELRAAGKKANK IGFFLHTPFPSSEIYRILPVRGQLLRGVLHCDLIGFHTYDYARHFLSSCS HLLGLVTTPSSVKYEGRSVAVGAFPIGIDPDKFTDGLKSPKVQNRIASLE NKFQGTKLMVSVDRLDYIKGIPQKLHALEVFLQNHPEWVGKVVLVQVAVP SRQDVEEYQNLRAVVNELVGRINGKFGTVDYMPIHFMHKSVSFDELIALY AASDACVVSSTRDGMNLVSFEYIATQQKRKGVLILSEFAGAAQSLNGSLV VNPWNTEELARAYHEAVSMSDEQRARKFEKLYKYISKYTSAFWGKSFVAE LLQC

Ligand information Ligand ID UDP InChI InChI=1S/C9H14N2O12P2/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(22-8)3-21-25(19,20)23-24(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1 InChIKey XCCTYIAWTASOJW-XVFCMESISA-N SMILES Software SMILES OpenEye OEToolkits 1.7.0 C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)OP(=O)(O)O)O)O CACTVS 3.370 O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O CACTVS 3.370 O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O OpenEye OEToolkits 1.7.0 C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)O)O)O ACDLabs 12.01 O=P(O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O Formula C9 H14 N2 O12 P2 Name URIDINE-5'-DIPHOSPHATE ChEMBL CHEMBL130266 DrugBank DB03435 ZINC ZINC000004490939 PDB chain 5hvo Chain B Residue 501 [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 5hvo Structural and In Vivo Studies on Trehalose-6-Phosphate Synthase from Pathogenic Fungi Provide Insights into Its Catalytic Mechanism, Biological Necessity, and Potential for Novel Antifungal Drug Design. Resolution 2.467 Å Binding residue (original residue number in PDB) V285 R287 K292 V322 S363 V364 L390 V391 E394 Binding residue (residue number reindexed from 1) V262 R264 K269 V299 S340 V341 L367 V368 E371 Annotation score 3

Enzymatic activity Catalytic site (original residue number in PDB) H179 D386 Catalytic site (residue number reindexed from 1) H156 D363 Enzyme Commision number 2.4.1.15: alpha,alpha-trehalose-phosphate synthase (UDP-forming).

Gene Ontology Molecular Function GO:0000166 nucleotide binding GO:0003824 catalytic activity GO:0003825 alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity GO:0004805 trehalose-phosphatase activity GO:0016757 glycosyltransferase activity GO:0016758 hexosyltransferase activity GO:0102986 trehalose synthase activity

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0005992	trehalose biosynthetic process
GO:0034605	cellular response to heat
GO:0070413	trehalose metabolism in response to stress

	Cellular Component
GO:0005946	alpha,alpha-trehalose-phosphate synthase complex (UDP-forming)

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