1R6T

crystal structure of human tryptophanyl-tRNA synthetase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001525	biological_process	angiogenesis
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004830	molecular_function	tryptophan-tRNA ligase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006436	biological_process	tryptophanyl-tRNA aminoacylation
A	0008285	biological_process	negative regulation of cell population proliferation
A	0016874	molecular_function	ligase activity
A	0019901	molecular_function	protein kinase binding
A	0019904	molecular_function	protein domain specific binding
A	0030674	molecular_function	protein-macromolecule adaptor activity
A	0032991	cellular_component	protein-containing complex
A	0035556	biological_process	intracellular signal transduction
A	0042803	molecular_function	protein homodimerization activity
A	0045765	biological_process	regulation of angiogenesis
A	0070062	cellular_component	extracellular exosome
B	0000166	molecular_function	nucleotide binding
B	0001525	biological_process	angiogenesis
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004830	molecular_function	tryptophan-tRNA ligase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006436	biological_process	tryptophanyl-tRNA aminoacylation
B	0008285	biological_process	negative regulation of cell population proliferation
B	0016874	molecular_function	ligase activity
B	0019901	molecular_function	protein kinase binding
B	0019904	molecular_function	protein domain specific binding
B	0030674	molecular_function	protein-macromolecule adaptor activity
B	0032991	cellular_component	protein-containing complex
B	0035556	biological_process	intracellular signal transduction
B	0042803	molecular_function	protein homodimerization activity
B	0045765	biological_process	regulation of angiogenesis
B	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TYM A 501

Chain	Residue
A	TYR159
A	GLU199
A	GLN284
A	ALA310
A	ASP312
A	GLN313
A	PHE317
A	PHE339
A	PHE340
A	LYS349
A	MSE350
A	THR160
A	HOH1002
A	HOH1007
A	HOH1018
A	HOH1028
A	HOH1044
A	HOH1113
A	GLY161
A	ARG162
A	GLY163
A	GLY172
A	HIS173
A	PRO176
A	GLN194

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 601

Chain	Residue
A	LYS253
A	ARG326
A	ILE327
B	TYR201
B	THR207
B	LEU208
B	HOH1138
B	HOH1213
B	HOH1285

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 602

Chain	Residue
A	ASP101
A	LYS111
A	GLY135
A	PHE138

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Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	11
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Ps.SEaMHVGHL

Chain	Residue	Details
A	PRO164-LEU174

---

site_id	PS00762
Number of Residues	29
Details	WHEP_TRS_1 WHEP-TRS domain signature. QGElVRslKagNAskdeIDsaVkmLvslK

Chain	Residue	Details
A	GLN19-LYS47

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P32921","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
A	ALA352
A	LYS349

---