Structure of PDB 4tvu Chain F

Receptor sequence
>4tvuF (length=548) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
PEWYKSAVFYELSVRTFQDGNGDGKGDFPGLTSRLDYLKNLGVDCLWLLP
WFPSPLRDDGYDVADYRGIHPDLGTLDDFKVFLREAHARGLWVIGDLVTN
HTSSDHPWFQAARRGPTLPDGSPNEYHDYYVWSDEGKEYADTRIIFTDTE
VSNWTLDEQAGKYYWHRFFASQPDLNYDNPKVVEELHGAARFWLDLGLDG
FRVDAVPYLIEREGTSCENLPETHEILKGFRAMVDREYPGRLLLAEANQW
PEEVVEYFGTEAEPEFHMCFNFPVMPRLYMSLKREDTSSIREIMGRLPKI
PSFGQWCIFLRNHDELTLEMVTDDERAFMYAAYAPDARMKINVGIRRRLA
PLLDNDRRRIELLNTVLLALPGSPVLYYGDEIGMGDDLGLPDRNGVRTPM
QWNAGTSGGFSTAQPSDCFFPPIQDPVYGFGRVNVQSQLQDPSSLLKWTA
RQLELRRAHPAFAHGDLTFIETGNPAILAFTRQYDGETLLIVSNFAGNAQ
AGLLDLAPFVGRAPVTLSGASPLPVVTGNGQYPVVMGKYDYYWLRLNS
3D structure
PDB4tvu Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization.
ChainF
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D101 R207 D209 E251 H318 D319
Catalytic site (residue number reindexed from 1) D96 R202 D204 E246 H313 D314
Enzyme Commision number 5.4.99.16: maltose alpha-D-glucosyltransferase.
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 CA F N105 D179 Y213 L214 E216 N100 D174 Y208 L209 E211
BS02 MG F D24 N26 D28 K30 D32 D19 N21 D23 K25 D27
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
GO:0047471 maltose alpha-D-glucosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4tvu, PDBe:4tvu, PDBj:4tvu
PDBsum4tvu
PubMed25478833
UniProtI3NX86

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