2ZXF

Crystal structure of human glycyl-trna synthetase (GLYRS) in complex with AP4A (cocrystallized with AP4A)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004081	molecular_function	bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004820	molecular_function	glycine-tRNA ligase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006426	biological_process	glycyl-tRNA aminoacylation
A	0015966	biological_process	diadenosine tetraphosphate biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016787	molecular_function	hydrolase activity
A	0030141	cellular_component	secretory granule
A	0030424	cellular_component	axon
A	0042802	molecular_function	identical protein binding
A	0042995	cellular_component	cell projection
A	0046983	molecular_function	protein dimerization activity
A	0070062	cellular_component	extracellular exosome
A	0070150	biological_process	mitochondrial glycyl-tRNA aminoacylation
A	0141192	molecular_function	ATP:ATP adenylyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE B4P A1101

Chain	Residue
A	PHE144
A	PHE292
A	MET294
A	ASN381
A	GLU403
A	ILE404
A	GLY406
A	SER524
A	GLY526
A	ARG529
A	ASP146
A	ARG159
A	ASP193
A	ARG277
A	GLU279
A	ILE287
A	ARG288
A	VAL289

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLN20-LYS48

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0000269|PubMed:24898252, ECO:0000305|PubMed:27261259, ECO:0007744|PDB:2ZT7, ECO:0007744|PDB:4KR3

Chain	Residue	Details
A	GLU245
A	GLU296

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0000305|PubMed:24898252, ECO:0000305|PubMed:27261259, ECO:0007744|PDB:2ZT7

Chain	Residue	Details
A	ARG277
A	GLU403

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0007744|PDB:2ZT7

Chain	Residue	Details
A	ARG288
A	ARG529

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:19710017, ECO:0000269|PubMed:24898252, ECO:0007744|PDB:2ZT7, ECO:0007744|PDB:4KR3

Chain	Residue	Details
A	GLU522

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS150
A	LYS447

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9CZD3

Chain	Residue	Details
A	TYR399

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CZD3

Chain	Residue	Details
A	SER646

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR682

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1qf6

Chain	Residue	Details
A	ARG277

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