Structure of PDB 7y1h Chain A

Receptor sequence

>7y1hA (length=487) Species: 9606 (Homo sapiens)

LEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFD
AEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEP
IAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTR
EFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEK
FAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEK
QFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGIALSE
EDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRL
EVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRAS
EDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARDQDM
GAKSLCIPFKPLCELQPGAKCVCKNPAKYYTLFGRSY

3D structure

• PDB: 7y1h Control of fibrosis with enhanced safety via asymmetric inhibition of prolyl-tRNA synthetase 1.
• Chain: A
• Resolution: 1.99 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	F99	A	H1093 F1097 P1120 T1121 E1123 R1152 H1173 H1242 S1272 W1273 G1274	H78 F82 P105 T106 E108 R137 H158 H227 S257 W258 G259
BS02	ATP	A	R1152 E1154 R1163 T1164 F1167 Q1237 G1239 T1240 T1276 R1278	R137 E139 R148 T149 F152 Q222 G224 T225 T261 R263
BS03	ZN	A	C1448 C1453 C1495	C431 C436 C471

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:7y1h, PDBe:7y1h, PDBj:7y1h
• PDBsum: 7y1h
• PubMed: 37212275
• UniProt: P07814|SYEP_HUMAN Bifunctional glutamate/proline--tRNA ligase (Gene Name=EPRS1)