Structure of PDB 5ykb Chain B

Receptor sequence
>5ykbB (length=522) Species: 243230 (Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539) [Search protein sequence]
PEWYKSAVFYELSVRTFQDGNGDGKGDFPGLTSRLDYLKNLGVDCLWLLP
WFPSPLRDDGYDVADYRGIHPDLGTLDDFKVFLREAHARGLWVIGDLVTN
HTSSDHPWFQAARRPNEYHDYYVWSDENWTLDEQAGKYYWHRFFASQPDL
NYDNPKVVEELHGAARFWLDLGLDGFRVDAVPYLIEREGTSCENLPETHE
ILKGFRAMVDREYPGRLLLAEAFQWPEEVVEYFGTEAEPEFHMCFNFPVM
PRLYMSLKREDTSSIREIMGRLPKIPSFGQWCIFLRNHDELTLEMVTDDE
RAFMYAAYAPDARMKINVGIRRRLAPLLDNDRRRIELLNTVLLALPGSPV
LYYGDEIGMGDDLGLPDRNGVRTPMQWNAGTSGGFSTAQPSDCFFPPIQD
PVYGFGRVNVQSQLQDPSSLLKWTARQLELRRAHPAFAHGDLTFIETGNP
AILAFTRQYDGETLLIVSNFAGNAQAGLLDLAPFVGRAPVTLSGASPLPV
VTGNGQYPVVMGKYDYYWLRLN
3D structure
PDB5ykb The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology
ChainB
Resolution2.76 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 R177 D179 E221 H288 D289
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 B N105 D179 L180 Y213 L214 E216 N100 D149 L150 Y183 L184 E186
BS02 MG B 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:5ykb, PDBe:5ykb, PDBj:5ykb
PDBsum5ykb
PubMed29095151
UniProtI3NX86

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