Structure of PDB 7y1w Chain A

Receptor sequence
>7y1wA (length=482) Species: 9606 (Homo sapiens) [Search protein sequence]
LEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFD
AEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEP
IAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTR
EFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEK
FAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEK
QFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGILSEE
DKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLE
VGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASE
DLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARMGAKS
LCIPFKPLCELQPGAKCVCNPAKYYTLFGRSY
3D structure
PDB7y1w Control of fibrosis with enhanced safety via asymmetric inhibition of prolyl-tRNA synthetase 1.
ChainA
Resolution2.5 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 ZN A C1448 C1495 C430 C467
BS02 F9O A F1097 E1100 P1120 T1121 E1123 R1152 E1171 H1173 H1242 W1273 G1274 F82 E85 P105 T106 E108 R137 E156 H158 H227 W258 G259
BS03 ATP A R1152 E1154 R1163 T1164 F1167 Q1237 G1239 T1240 T1276 R1278 R137 E139 R148 T149 F152 Q222 G224 T225 T261 R263
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:7y1w, PDBe:7y1w, PDBj:7y1w
PDBsum7y1w
PubMed37212275
UniProtP07814|SYEP_HUMAN Bifunctional glutamate/proline--tRNA ligase (Gene Name=EPRS1)

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