Structure of PDB 5hvm Chain A Binding Site BS01

Receptor Information
>5hvm Chain A (length=446) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ARLLLVSNRLPIYDFSMSGGLVSGFQWYGWPGLEVPEPVVKQRLKDEYGA
IPVFIDDELADRHYNGFSNSILWPLFHYHPGEITFDESAWEAYKEANRLF
AKAVAKEVQDGDLIWVHDYHLMLLPEMLREEIGDSKENVKIGFFLHTPFP
SSEIYRILPVRNELLLGVLHCDLIGFHTYDYTRHFLSACSRLLGLATTPN
GIEFQGKVIACGAFPIGIDPEKFQEGLKKEKVQKRIAQLEQKFQGVKLMV
GVDRLDYIKGVPQKLHALEVFLSDHPEWVGKVVLVQVAVPSRQDVEEYQN
LRAVVNELVGRINGKFGTVEFMPIHFLHKSVNFDELIALYAVSDACIVSS
TRDGMNLVAYEYIASQQKRHGVLVLSEFAGAAQSLNGSIIINPWNTEELA
GAYQEAVTMSDEQRALNFSKLDKYVNKYTSAFWGQSFVTELNRISA
Ligand information
Ligand IDUDP
InChIInChI=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
InChIKeyXCCTYIAWTASOJW-XVFCMESISA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C1=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 3.370O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
CACTVS 3.370O[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 1.7.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)O)O)O
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O
FormulaC9 H14 N2 O12 P2
NameURIDINE-5'-DIPHOSPHATE
ChEMBLCHEMBL130266
DrugBankDB03435
ZINCZINC000004490939
PDB chain5hvm Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5hvm 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.
Resolution2.815 Å
Binding residue
(original residue number in PDB)		V285 R287 K292 V322 S363 V364 L390 V391 E394
Binding residue
(residue number reindexed from 1)		V252 R254 K259 V289 S330 V331 L357 V358 E361
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) H179 D386
Catalytic site (residue number reindexed from 1) H146 D353
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5hvm, PDBe:5hvm, PDBj:5hvm
PDBsum5hvm
PubMed28743811
UniProtQ4WLM9|TPS1A_ASPFU Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1 (Gene Name=tpsA)

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