2PME

The Apo crystal Structure of the glycyl-tRNA synthetase

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	0016874	molecular_function	ligase 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 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 site: {"evidences":[{"source":"PubMed","id":"19710017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24898252","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27261259","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2ZT7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KR3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19710017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24898252","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27261259","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2ZT7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19710017","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZT7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19710017","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24898252","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZT7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KR3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9CZD3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CZD3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG277

---