Structure of PDB 5huu Chain A Binding Site BS02

Receptor Information
>5huu Chain A (length=469) 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
YTSGFWGESFVKELYKCNP
Ligand information
Ligand IDG6P
InChIInChI=1S/C6H13O9P/c7-3-2(1-14-16(11,12)13)15-6(10)5(9)4(3)8/h2-10H,1H2,(H2,11,12,13)/t2-,3-,4+,5-,6+/m1/s1
InChIKeyNBSCHQHZLSJFNQ-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)OP(=O)(O)O
CACTVS 3.341O[CH]1O[CH](CO[P](O)(O)=O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341O[C@H]1O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H](O)[C@H]1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)OP(=O)(O)O
ACDLabs 10.04O=P(O)(O)OCC1OC(O)C(O)C(O)C1O
FormulaC6 H13 O9 P
Name6-O-phosphono-alpha-D-glucopyranose;
ALPHA-D-GLUCOSE-6-PHOSPHATE;
6-O-phosphono-alpha-D-glucose;
6-O-phosphono-D-glucose;
6-O-phosphono-glucose
ChEMBL
DrugBankDB02007
ZINCZINC000003875375
PDB chain5huu Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5huu 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.
Resolution2.37 Å
Binding residue
(original residue number in PDB)		Y89 D143 R318
Binding residue
(residue number reindexed from 1)		Y86 D140 R315
Annotation score5
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5huu, PDBe:5huu, PDBj:5huu
PDBsum5huu
PubMed28743811
UniProtQ92410|TPS1_CANAL Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (Gene Name=TPS1)

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