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Structure of PDB 5hvl Chain B Binding Site BS01

Receptor Information >5hvl Chain B (length=466) Species: 237561 (Candida albicans SC5314) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] GKVLVVSNRIPVTIKRLDNGSYDYSMSSGGLVTALQGLKKTTEFQWYGWP GLEIPEDEQTKVNDELKSKFNCTAIFLSDTIADLHYNGFSNSILWPLFHY HPGEMNFDENAWAAYIEANKKFALEIVKQVNDDDMIWVHDYHLMLLPEML RQEIGNKKKNIKIGFFLHTPFPSSEIYRILPVRKEILEGVLSCDLIGFHT YDYARHFISSVSRIVPNVSTLPNGIKYQGRSISIGAFPIGIDVDNFIDGL KKDSVVERIKQLKSKFKDVKVIVGVDRLDYIKGVPQKLHAFEVFLNENPE WIGKVVLVQVAVPSRGDVEEYQSLRSTVSELVGRINGEFGTVEFVPIHYL HKSIPFDELISLYNISDVCLVSSTRDGMNLVSYEYIACQQDRKGVLILSE FAGAAQSLNGALIVNPWNTEDLSEAIKESLTLPEEKREFNFKKLFTYISK YTSGFWGESFVKELYK

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 5hvl 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 5hvl 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 1.796 Å Binding residue (original residue number in PDB) V278 R280 K285 V315 S356 I357 L362 L383 V384 E387 Binding residue (residue number reindexed from 1) V275 R277 K282 V312 S353 I354 L359 L380 V381 E384 Annotation score 3

Enzymatic activity Catalytic site (original residue number in PDB) H171 D379 Catalytic site (residue number reindexed from 1) H168 D376 Enzyme Commision number 2.4.1.15: alpha,alpha-trehalose-phosphate synthase (UDP-forming).

Gene Ontology Molecular Function 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

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0005992	trehalose biosynthetic process
GO:0006623	protein targeting to vacuole
GO:0030447	filamentous growth
GO:0033554	cellular response to stress
GO:0034605	cellular response to heat
GO:0034727	piecemeal microautophagy of the nucleus
GO:0036168	filamentous growth of a population of unicellular organisms in response to heat
GO:0036180	filamentous growth of a population of unicellular organisms in response to biotic stimulus
GO:0070413	trehalose metabolism in response to stress
GO:0071465	cellular response to desiccation

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

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