Structure of PDB 4k87 Chain A

Receptor sequence

>4k87A (length=490) Species: 9606 (Homo sapiens)

LEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFD
AEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEP
IAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTR
EFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEK
FAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEK
QFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNAL
SEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPI
RLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTR
ASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARDQ
SMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY

3D structure

• PDB: 4k87 Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone.
• Chain: A
• Resolution: 2.301 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	ZN	A	C448 C453 C495 C497	C433 C438 C473 C475
BS02	ADN	A	R163 F167 Q237 T276 R278	R148 F152 Q222 T261 R263
BS03	PRO	A	T121 E123 W169 E171 H173 F216 H242 S272 W273	T106 E108 W154 E156 H158 F201 H227 S257 W258

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:4k87, PDBe:4k87, PDBj:4k87
• PDBsum: 4k87
• PubMed: 24100331
• UniProt: P07814|SYEP_HUMAN Bifunctional glutamate/proline--tRNA ligase (Gene Name=EPRS1)