4G85

Crystal structure of human HisRS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004821	molecular_function	histidine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006427	biological_process	histidyl-tRNA aminoacylation
A	0032543	biological_process	mitochondrial translation
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
B	0003723	molecular_function	RNA binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004821	molecular_function	histidine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006427	biological_process	histidyl-tRNA aminoacylation
B	0032543	biological_process	mitochondrial translation
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLN14-LYS42

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:25151410, ECO:0007744|PDB:4PHC

Chain	Residue	Details
A	ASP130
B	ASP177
B	ARG326
B	TYR330
A	ARG157
A	GLN173
A	ASP177
A	ARG326
A	TYR330
B	ASP130
B	ARG157
B	GLN173

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330

Chain	Residue	Details
A	ALA2
B	ALA2

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99KK9

Chain	Residue	Details
A	SER66
B	SER66

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER356
B	SER356

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