6ENG

Crystal structure of the 43K ATPase domain of Escherichia coli gyrase B in complex with an aminocoumarin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A	0005524	molecular_function	ATP binding
A	0006265	biological_process	DNA topological change
B	0003677	molecular_function	DNA binding
B	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B	0005524	molecular_function	ATP binding
B	0006265	biological_process	DNA topological change

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue PO4 A 401

Chain	Residue
A	ARG192
A	TYR228
A	LYS231

---

site_id	AC2
Number of Residues	5
Details	binding site for residue PO4 A 402

Chain	Residue
A	HIS64
A	ARG168
A	LYS208
A	HOH514
A	HOH531

---

site_id	AC3
Number of Residues	8
Details	binding site for residue PG4 A 403

Chain	Residue
A	ASN265
A	ILE266
A	TYR267
A	CYS268
A	ARG276
A	LEU282
A	HOH557
A	GLU264

---

site_id	AC4
Number of Residues	2
Details	binding site for residue CL A 404

Chain	Residue
A	ARG204
A	HIS215

---

site_id	AC5
Number of Residues	6
Details	binding site for residue NA A 405

Chain	Residue
A	ILE273
A	PRO274
A	THR336
A	LYS337
A	ASP338
A	HOH695

---

site_id	AC6
Number of Residues	4
Details	binding site for residue K A 406

Chain	Residue
A	GLY102
A	LYS103
A	ASP105
A	HOH543

---

site_id	AC7
Number of Residues	5
Details	binding site for residue K A 407

Chain	Residue
A	ASN271
A	ILE273
A	HOH589
A	HOH599
A	HOH621

---

site_id	AC8
Number of Residues	4
Details	binding site for residue K A 408

Chain	Residue
A	TYR242
A	HOH640
A	HOH682
A	HOH689

---

site_id	AC9
Number of Residues	33
Details	binding site for residue BHW B 401

Chain	Residue
A	ASN46
A	GLU50
A	VAL71
A	ASP73
A	ARG76
A	GLY77
A	ILE78
A	ILE94
A	GLY101
A	PHE104
A	ASP105
A	LYS110
A	VAL120
A	ARG136
B	VAL43
B	ASN46
B	GLU50
B	VAL71
B	ASP73
B	ARG76
B	GLY77
B	ILE78
B	ILE94
B	GLY101
B	PHE104
B	ASP105
B	LYS110
B	VAL120
B	ARG136
B	THR165
B	HOH524
B	HOH557
B	HOH608

---

site_id	AD1
Number of Residues	3
Details	binding site for residue PO4 B 402

Chain	Residue
B	ARG192
B	TYR228
B	LYS231

---

site_id	AD2
Number of Residues	7
Details	binding site for residue PO4 B 403

Chain	Residue
B	HIS64
B	ARG168
B	LYS208
B	HOH506
B	HOH548
B	HOH560
B	HOH603

---

site_id	AD3
Number of Residues	2
Details	binding site for residue PO4 B 404

Chain	Residue
B	LYS223
B	TYR242

---

site_id	AD4
Number of Residues	2
Details	binding site for residue CL B 405

Chain	Residue
B	ARG204
B	HIS215

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor (ATPase activity) => ECO:0000305|PubMed:10734094, ECO:0000305|PubMed:8248233

Chain	Residue	Details
A	GLU42
B	GLU42

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:25202966, ECO:0000269|PubMed:25849408, ECO:0000305|PubMed:10734094

Chain	Residue	Details
A	TYR5
B	TYR5

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:10734094, ECO:0000269|PubMed:25202966, ECO:0000269|PubMed:25849408

Chain	Residue	Details
A	ASN46
B	LEU115
A	ASP73
A	GLY102
A	TYR109
A	LEU115
B	ASN46
B	ASP73
B	GLY102
B	TYR109

---

site_id	SWS_FT_FI4
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269|PubMed:25849408

Chain	Residue	Details
A	ILE94
B	ALA100
B	LYS103
B	ASP105
B	GLY117
B	SER121
A	VAL97
A	ALA100
A	LYS103
A	ASP105
A	GLY117
A	SER121
B	ILE94
B	VAL97

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10734094, ECO:0000269|PubMed:25849408

Chain	Residue	Details
A	GLN335
B	GLN335

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:9657678

Chain	Residue	Details
A	LYS337
B	LYS337

---