Structure of PDB 6rlt Chain B

Receptor sequence
>6rltB (length=456) Species: 31285 (Trypanosoma brucei gambiense) [Search protein sequence]
MVLDIQLFRDETGANIIRESQRRRFADPDIVDAIIEADKKWRRTQFLTEA
SKKLINICSKAVGAKKKAKEADGDTSEIPPQVKEAYENGTLKGEQVEQLC
VLQLKQLSKDLSDQVAGLAKEAQQLEEERDKLMLNVGNILHESVPIAQDE
ETGNTVVRTFGNTTKRAKLNHVSIMERLGMMDTSKAVTSMAGGRSYVLKG
GLVQLQVALVSYSLDFLVKRGYTPFYPPFFLNRDVMGEVAQLSQFDEELY
QVSGDKKYLIATSEMPIAAYHRGRWFTELKEPLKYAGMSTCFRKEALGIF
RVHQFDKIEQFVVCSPRQEESWRHLEDMITTSEEFNKSLGLPYRVVNICS
GALNNAAAKKYDLEAWFPASGAFRELVSCSNCTDYQSQSVNCRYGPNLRG
TAAQNVKEYCHMLNGTLCAITRTMCCICENYQTEEGVVIPDVLRPYMMGI
EMIRFE
3D structure
PDB6rlt Structural Insights into the Binding of Natural Pyrimidine-Based Inhibitors of Class II Aminoacyl-tRNA Synthetases.
ChainB
Resolution1.84 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.11: serine--tRNA ligase.
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 FZK B T264 E266 R295 E297 V311 F314 K316 E318 E384 L385 V386 S387 N423 T425 A428 R431 T262 E264 R293 E295 V302 F305 K307 E309 E375 L376 V377 S378 N414 T416 A419 R422
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004828 serine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006434 seryl-tRNA aminoacylation
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6rlt, PDBe:6rlt, PDBj:6rlt
PDBsum6rlt
PubMed31869198
UniProtD0A7P1

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