4HWP

Crystal structure of E. coli Threonyl-tRNA synthetase bound to a novel inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004829	molecular_function	threonine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006435	biological_process	threonyl-tRNA aminoacylation
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004829	molecular_function	threonine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006435	biological_process	threonyl-tRNA aminoacylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 701

Chain	Residue
A	CYS334
A	HIS385
A	HIS511

---

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE X16 A 702

Chain	Residue
A	VAL376
A	PHE379
A	GLN381
A	ASP383
A	HIS385
A	TYR462
A	LYS465
A	GLN479
A	THR482
A	GLN484
A	HIS511
A	GLY516
A	SER517
A	ARG520
A	ZN701
A	HOH828
A	HOH871
A	HOH1032
A	MET332
A	CYS334
A	ARG363
A	GLU365
A	MET374
A	ARG375

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 701

Chain	Residue
B	CYS334
B	HIS385
B	HIS511

---

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE X16 B 702

Chain	Residue
B	MET332
B	CYS334
B	ARG363
B	GLU365
B	MET374
B	ARG375
B	VAL376
B	PHE379
B	GLN381
B	ASP383
B	HIS385
B	TYR462
B	LYS465
B	GLN479
B	GLN484
B	HIS511
B	SER517
B	ARG520
B	ZN701
B	HOH826
B	HOH931
B	HOH1042

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:11953757

Chain	Residue	Details
B	LYS246
B	ASN342
B	LEU489
B	ASP615
A	ASN342
A	LEU489
A	ASP615
A	LYS246

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:10319817, ECO:0007744|PDB:1QF6

Chain	Residue	Details
A	GLN381
A	GLN479
A	SER517
B	HIS309
B	VAL376
B	GLN381
B	GLN479
B	SER517
A	HIS309
A	VAL376

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:10319817

Chain	Residue	Details
A	TYR348
A	ARG363
A	ARG375
A	PHE379
A	TYR462
A	GLN484
A	ARG520
A	ILE547
A	ASN575
A	ARG589
A	VAL595
A	ARG609
B	TYR313
B	ARG325
B	TYR348
B	ARG363
B	ARG375
B	PHE379
B	TYR462
B	GLN484
B	ARG520
B	ILE547
B	ASN575
B	ARG589
B	VAL595
B	ARG609
A	TYR313
A	ARG325

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973, ECO:0000269|PubMed:11953757

Chain	Residue	Details
B	CYS334
B	HIS385
A	CYS334
A	HIS385

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973

Chain	Residue	Details
A	HIS511
B	HIS511

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_00184, ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	LYS286
B	LYS286

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 540

Chain	Residue	Details
A	CYS334	electrostatic stabiliser, metal ligand
A	ARG363	electrostatic stabiliser
A	GLN381	electrostatic stabiliser
A	ASP383	electrostatic stabiliser
A	HIS385	metal ligand
A	LYS465	electrostatic stabiliser
A	HIS511	metal ligand

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 540

Chain	Residue	Details
B	CYS334	electrostatic stabiliser, metal ligand
B	ARG363	electrostatic stabiliser
B	GLN381	electrostatic stabiliser
B	ASP383	electrostatic stabiliser
B	HIS385	metal ligand
B	LYS465	electrostatic stabiliser
B	HIS511	metal ligand

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