Structure of PDB 7osy Chain B

Receptor sequence
>7osyB (length=484) Species: 9606 (Homo sapiens) [Search protein sequence]
LEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFD
AEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEP
IAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTR
EFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEK
FAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEK
QFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGILSEE
DKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLE
VGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASE
DLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARMGAKS
LCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY
3D structure
PDB7osy Towards Novel 3-Aminopyrazinamide-Based Prolyl-tRNA Synthetase Inhibitors: In Silico Modelling, Thermal Shift Assay and Structural Studies.
ChainB
Resolution2.23 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.15: proline--tRNA ligase.
6.1.1.17: glutamate--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 PRO B T1121 E1123 R1152 W1169 E1171 H1173 F1216 H1242 W1273 G1274 T106 E108 R137 W154 E156 H158 F201 H227 W258 G259
BS02 ZN B C1448 C1453 C1495 C1497 C430 C435 C467 C469
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004827 proline-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006433 prolyl-tRNA aminoacylation
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:7osy, PDBe:7osy, PDBj:7osy
PDBsum7osy
PubMed34360555
UniProtP07814|SYEP_HUMAN Bifunctional glutamate/proline--tRNA ligase (Gene Name=EPRS1)

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