1O0C

CRYSTAL STRUCTURE OF L-GLUTAMATE AND AMPCPP BOUND TO GLUTAMINE AMINOACYL TRNA SYNTHETASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004819	molecular_function	glutamine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
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	0006424	biological_process	glutamyl-tRNA aminoacylation
A	0006425	biological_process	glutaminyl-tRNA aminoacylation
A	0043039	biological_process	tRNA aminoacylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1394

Chain	Residue
A	HIS40
A	HIS43
A	ARG260
A	MET268
A	LYS270
A	AMP998

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1395

Chain	Residue
A	LYS272
A	GLY482
A	VAL267
A	MET268
A	SER269

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GLU A 996

Chain	Residue
A	ARG30
A	PRO32
A	ASP66
A	TYR211
A	HIS215
A	LEU228
A	CYS229
A	PHE233
A	AMP998
A	HOH1396
A	HOH1475
A	HOH1479
B	A976

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AMP A 998

Chain	Residue
A	PHE31
A	PRO33
A	GLU34
A	HIS40
A	GLY42
A	HIS43
A	SER46
A	ARG260
A	LEU261
A	LYS270
A	GLU996
A	SO41394
A	HOH1445
A	HOH1475
A	HOH1479
B	A976

---

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	12
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PepNGyLHIGHA

Chain	Residue	Details
A	PRO33-ALA44

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:23727144, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ

Chain	Residue	Details
A	PRO35
A	ILE41

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B

Chain	Residue	Details
A	ASP67

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:12691748, ECO:0000269|PubMed:15845536, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:1O0B, ECO:0007744|PDB:1ZJW

Chain	Residue	Details
A	ASP212

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00126, ECO:0000269|PubMed:18477696, ECO:0000269|PubMed:23727144, ECO:0000269|PubMed:9562563, ECO:0007744|PDB:4JXX, ECO:0007744|PDB:4JXZ, ECO:0007744|PDB:4JYZ

Chain	Residue	Details
A	LEU261
A	SER269
A	LEU231

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 850

Chain	Residue	Details
A	PRO35	proton shuttle (general acid/base)
A	LEU261	electrostatic stabiliser
A	ARG271	electrostatic stabiliser

---