Structure of PDB 5nfh Chain A

Receptor sequence
>5nfhA (length=519) Species: 185431 (Trypanosoma brucei brucei TREU927) [Search protein sequence]
VEKVFFVTSPIYYVNAAPHIGHVYSTLITDVIGRYHRVKGERVFALTGTD
EHGQKVAEAAKQKQVSPYDFTTAVAGEFKKCFEQMDYSIDYFIRTTNEQH
KAVVKELWTKLEQKGDIYLGRYEGWYSISDESFLTPQNITDGVDKDGNPC
KVSLESGHVVTWVSEENYMFRLSAFRERLLEWYHANPGCIVPEFRRREVI
RAVEKGLPDLSVSRARATLHNWAIPVPGNPDHCVYVWLDALTNYLTGSRL
RVDESGKEVSLVDDFNELERFPADVHVIGKDILKFHAIYWPAFLLSAGLP
LPKKIVAHGWWTKDVFDPVEKAEEFGYDALKYFLLRESGFSDDGDYSDKN
MIARLNGELADTLGNLVMRCTSAKINVNGEWPSPAAYTEEDESLIQLIKD
LPGTADHYYLIPDIQKAIIAVFDVLRAINAYVTDMAPWKLVKTDPERLRT
VLYITLEGVRVTTLLLSPILPRKSVVIFDMLGVPEVHRKGIENFEFGAVP
PGTRLGPAVEGEVLFSKRS
3D structure
PDB5nfh Chemical Validation of Methionyl-tRNA Synthetase as a Druggable Target in Leishmania donovani.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H256 H259 S364 D367 S390 S393
Catalytic site (residue number reindexed from 1) H19 H22 S127 D130 S153 S156
Enzyme Commision number 6.1.1.10: methionine--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 MET A P247 I248 Y250 D287 W474 K550 P10 I11 Y13 D50 W237 K313
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004825 methionine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006431 methionyl-tRNA aminoacylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5nfh, PDBe:5nfh, PDBj:5nfh
PDBsum5nfh
PubMed28967262
UniProtQ38C91

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