Structure of PDB 5l3k Chain A

Receptor sequence
>5l3kA (length=448) Species: 1797 (Mycolicibacterium thermoresistibile) [Search protein sequence]
SDFVVVANRLPIDLRSPGGLVTALEPLLRRAWIGWPGIPDSDEDPVLYPV
RLSADDVAQYYEGFSNATLWPLYHDVIVKPIYNRQWWERYVEVNRRFAEA
TSRAAARGATVWVQDYQLQLVPKMLRELRPDLTIGFFLHIPFPPVELFMQ
LPWRTEITDGLLGADLVGFHLPGGAQNFLFLARRLVGANTSRASVGVRSK
FGEVQIGSRTVKVGAFPISIDSADLDRQARQRSIRQRARQIRAELGNPRR
ILLGVDRLDYTKGIDVRLQAFAELLAEGRVNREDTVFVQLATPSRERVEA
YRLLRDDIERQVGHINGEYGEVGHPVVHYLHRPVPREELIAFFVAADVML
VTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELGQAYLVNPHNLD
HVKDTMVAALNQTPEEGRRRMRALRRQVLAHDVDLWARSFLDALASTR
3D structure
PDB5l3k Mycobacterial OtsA Structures Unveil Substrate Preference Mechanism and Allosteric Regulation by 2-Oxoglutarate and 2-Phosphoglycerate.
ChainA
Resolution2.305 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H168 D385
Catalytic site (residue number reindexed from 1) H139 D356
Enzyme Commision number 2.4.1.347: alpha,alpha-trehalose-phosphate synthase (ADP-forming).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP A G38 G39 D285 R286 K291 L319 T321 V363 N388 L389 V390 E393 G18 G19 D256 R257 K262 L290 T292 V334 N359 L360 V361 E364
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005992 trehalose biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5l3k, PDBe:5l3k, PDBj:5l3k
PDBsum5l3k
PubMed31772052
UniProtA0A117IMA6

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