Structure of PDB 7y3s Chain B

Receptor sequence

>7y3sB (length=483) Species: 9606 (Homo sapiens)

GLEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFF
DAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAE
PIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRT
REFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKE
KFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGE
KQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGISEE
DKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLE
VGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASE
DLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTAMGAKSL
CIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY

3D structure

• PDB: 7y3s Control of fibrosis with enhanced safety via asymmetric inhibition of prolyl-tRNA synthetase 1.
• Chain: B
• Resolution: 2.6 Å

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	F9C	B	H1093 F1097 T1121 E1123 R1152 T1240 H1242 W1273 G1274	H79 F83 T107 E109 R138 T226 H228 W259 G260
BS02	ATP	B	R1152 E1154 L1162 R1163 T1164 F1167 Q1237 G1239 T1240 T1276 R1278	R138 E140 L148 R149 T150 F153 Q223 G225 T226 T262 R264
BS03	ZN	B	C1448 C1453 C1495 C1497	C430 C435 C466 C468

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

External links

• PDB: RCSB:7y3s, PDBe:7y3s, PDBj:7y3s
• PDBsum: 7y3s
• PubMed: 37212275
• UniProt: P07814|SYEP_HUMAN Bifunctional glutamate/proline--tRNA ligase (Gene Name=EPRS1)