4HYP

Pyrrolopyrimidine inhibitors of dna gyrase b and topoisomerase iv, part i: structure guided discovery and optimization of dual targeting agents with potent, broad-spectrum enzymatic activity.

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
C	0003677	molecular_function	DNA binding
C	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
C	0005524	molecular_function	ATP binding
C	0006265	biological_process	DNA topological change
D	0003677	molecular_function	DNA binding
D	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
D	0005524	molecular_function	ATP binding
D	0006265	biological_process	DNA topological change

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 1A1 A 301

Chain	Residue
A	VAL43
A	ILE94
A	PHE104
A	ARG140
A	THR169
A	HOH426
A	HOH436
A	ASN46
A	GLU50
A	VAL71
A	ASP73
A	ARG76
A	GLY77
A	ILE78
A	PRO79

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 302

Chain	Residue
A	GLU42
A	ASP45
A	GLY118
A	LEU119
A	VAL122
A	HOH465

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 1A1 B 301

Chain	Residue
B	VAL43
B	ASN46
B	ALA47
B	GLU50
B	VAL71
B	ASP73
B	ARG76
B	GLY77
B	ILE78
B	PRO79
B	ILE94
B	PHE104
B	ARG140
B	THR169
B	HOH420
B	HOH440
B	HOH479

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 302

Chain	Residue
B	GLU42
B	ASP45
B	VAL122
B	HOH472
B	HOH473

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 1A1 C 301

Chain	Residue
C	VAL43
C	ASN46
C	GLU50
C	VAL71
C	ASP73
C	ARG76
C	GLY77
C	ILE78
C	PRO79
C	ILE94
C	PHE104
C	ARG140
C	THR169
C	HOH416
C	HOH428
C	HOH437
C	HOH478

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 302

Chain	Residue
C	GLU42
C	ASP45
C	LEU119
C	VAL122
C	HOH477

---

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1A1 D 301

Chain	Residue
D	VAL43
D	ASN46
D	ALA47
D	GLU50
D	ASP73
D	ARG76
D	ILE78
D	PRO79
D	ARG140
D	THR169
D	HOH402
D	HOH407
D	HOH441
D	HOH456

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 302

Chain	Residue
D	GLU42
D	ASP45
D	VAL122
D	HOH472

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor (ATPase activity) => ECO:0000305|PubMed:10734094, ECO:0000305|PubMed:8248233

Chain	Residue	Details
A	GLU42
B	GLU42
C	GLU42
D	GLU42

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:10734094, ECO:0000269|PubMed:25202966, ECO:0000269|PubMed:25849408

Chain	Residue	Details
A	ASN46
B	LEU119
C	ASN46
C	ASP73
C	GLY102
C	TYR113
C	LEU119
D	ASN46
D	ASP73
D	GLY102
D	TYR113
A	ASP73
D	LEU119
A	GLY102
A	TYR113
A	LEU119
B	ASN46
B	ASP73
B	GLY102
B	TYR113

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:25849408

Chain	Residue	Details
A	ILE94
B	ALA100
B	LYS103
B	ASP109
B	GLY121
B	SER125
C	ILE94
C	VAL97
C	ALA100
C	LYS103
C	ASP109
A	VAL97
C	GLY121
C	SER125
D	ILE94
D	VAL97
D	ALA100
D	LYS103
D	ASP109
D	GLY121
D	SER125
A	ALA100
A	LYS103
A	ASP109
A	GLY121
A	SER125
B	ILE94
B	VAL97

---