6KID

Crystal structure of human leucyl-tRNA synthetase, ATP-bound form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0002161	molecular_function	aminoacyl-tRNA deacylase activity
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004819	molecular_function	glutamine-tRNA ligase activity
A	0004823	molecular_function	leucine-tRNA ligase activity
A	0005096	molecular_function	GTPase activator activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006425	biological_process	glutaminyl-tRNA aminoacylation
A	0006429	biological_process	leucyl-tRNA aminoacylation
A	0012505	cellular_component	endomembrane system
A	0016874	molecular_function	ligase activity
A	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
A	0034198	biological_process	cellular response to amino acid starvation
A	0071230	biological_process	cellular response to amino acid stimulus
A	0071233	biological_process	cellular response to L-leucine
A	0106074	biological_process	aminoacyl-tRNA metabolism involved in translational fidelity
A	1904263	biological_process	positive regulation of TORC1 signaling
A	1990253	biological_process	cellular response to leucine starvation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue ATP A 1201

Chain	Residue
A	PHE50
A	SER673
A	GLY674
A	ASP676
A	LEU677
A	HIS709
A	LEU710
A	HOH1353
A	HOH1376
A	HOH1382
A	PRO51
A	TYR52
A	PRO53
A	TYR54
A	GLY62
A	HIS63
A	SER66
A	GLU257

---

site_id	AC2
Number of Residues	7
Details	binding site for residue LEU A 1202

Chain	Residue
A	THR293
A	LEU294
A	VAL389
A	THR390
A	SER396
A	ASP399
A	TYR468

---

site_id	AC3
Number of Residues	4
Details	binding site for residue PO4 A 1203

Chain	Residue
A	THR255
A	GLY256
A	HOH1359
A	HOH1391

---

site_id	AC4
Number of Residues	2
Details	binding site for residue PO4 A 1204

Chain	Residue
A	ASN56
A	ARG517

---

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	12
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PymNGrLHLGHT

Chain	Residue	Details
A	PRO53-THR64

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	249
Details	Region: {"description":"Editing domain","evidences":[{"source":"PubMed","id":"19426743","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Motif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Motif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMJ2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---