5E6M

Crystal structure of human wild type GlyRS bound with tRNAGly

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	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
B	0000166	molecular_function	nucleotide binding
B	0004081	molecular_function	bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004820	molecular_function	glycine-tRNA ligase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006426	biological_process	glycyl-tRNA aminoacylation
B	0015966	biological_process	diadenosine tetraphosphate biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016787	molecular_function	hydrolase activity
B	0016874	molecular_function	ligase activity
B	0030141	cellular_component	secretory granule
B	0030424	cellular_component	axon
B	0042802	molecular_function	identical protein binding
B	0046983	molecular_function	protein dimerization activity
B	0070062	cellular_component	extracellular exosome
B	0070150	biological_process	mitochondrial glycyl-tRNA aminoacylation
B	0141192	molecular_function	ATP:ATP adenylyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue GAP A 701

Chain	Residue
A	GLU245
A	ILE404
A	GLY406
A	ARG410
A	GLU522
A	SER524
A	GLY526
A	ARG529
E	A76
A	ARG277
A	GLU279
A	ILE287
A	ARG288
A	VAL289
A	PHE292
A	GLU296
A	GLU403

---

site_id	AC2
Number of Residues	8
Details	binding site for residue SO4 A 702

Chain	Residue
A	TYR94
A	LYS104
A	ASN274
A	GLU291
A	THR293
B	ASP125
B	CYS126
B	THR127

---

site_id	AC3
Number of Residues	17
Details	binding site for residue GAP B 701

Chain	Residue
B	GLU245
B	ARG277
B	GLU279
B	LEU286
B	ILE287
B	ARG288
B	VAL289
B	PHE292
B	GLU296
B	GLU403
B	ILE404
B	GLU522
B	SER524
B	GLY526
B	ARG529
B	HOH802
C	A76

---

site_id	AC4
Number of Residues	3
Details	binding site for residue NI C 101

Chain	Residue
C	U8
C	G9
C	G12

---

site_id	AC5
Number of Residues	3
Details	binding site for residue NI E 101

Chain	Residue
E	U8
E	G9
E	G12

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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	6
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	4
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	4
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	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9CZD3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CZD3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---