Structure of PDB 3sgl Chain A

Receptor sequence
>3sglA (length=630) Species: 632 (Yersinia pestis) [Search protein sequence]
GLEETHHVFLKGNGFPARFASHPQQSCIFAETGFGTGLNFLTLWRDFALF
RQQSPNATLRRLHYISFEKYPLHVADLASAHARWPELASFAEQLRAQWPL
PLAGCHRILLADGAITLDLWFGDVNTLLPTLDDSLNNQVDAWFLDGFAPA
KNPDMWNEQLFNAMARMTRPGGTFSTFTAAGFVRRGLQQAGFNVTKVKGF
GQKREMLTGTLPQQIHAPTAPWYHRPAATRCDDIAIIGGGIVSALTALAL
QRRGAVVTLYCADAQPAQGASGNRQGALYPLLNGKNDALETFFTSAFTFA
RRQYDQLLEQGIAFDHQWCGVSQLAFDDKSRGKIEKMLHTQWPVEFAEAM
SREQLSELAGLDCAHDGIHYPAGGWLCPSDLTHALMMLAQQNGMTCHYQH
ELQRLKRIDSQWQLTFGQAAKHHATVILATGHRLPEWEQTHHLPLSAVRG
QVSHIPTTPVLSQLQQVLCYDGYLTPVNPANQHHCIGASYQRGDIATDFR
LTEQQENRERLLRCLPQVSWPQQVDVSDNQARCGVRCAIRDHLPMVGAVP
DYAATLAQYQDLSRRIDIAVAPVWPELFMVGGLGSRGLCSAPLVAEILAA
QMFGEPLPLDAKTLAALNPNRFWIRKLLKG
3D structure
PDB3sgl Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC.
ChainA
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.5.-.-
2.1.1.61: tRNA 5-(aminomethyl)-2-thiouridylate-methyltransferase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004808 tRNA (5-methylaminomethyl-2-thiouridylate)(34)-methyltransferase activity
GO:0008168 methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0016491 oxidoreductase activity
GO:0016645 oxidoreductase activity, acting on the CH-NH group of donors
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0002097 tRNA wobble base modification
GO:0002098 tRNA wobble uridine modification
GO:0008033 tRNA processing
GO:0032259 methylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3sgl, PDBe:3sgl, PDBj:3sgl
PDBsum3sgl
PubMed23617613
UniProtQ8ZD36|MNMC_YERPE tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC (Gene Name=mnmC)

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