4DDQ

Structural plasticity of the Bacillus subtilis GyrA homodimer

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	0006259	biological_process	DNA metabolic process
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	0006259	biological_process	DNA metabolic process
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	0006259	biological_process	DNA metabolic process
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	0006259	biological_process	DNA metabolic process
D	0006265	biological_process	DNA topological change
E	0003677	molecular_function	DNA binding
E	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
E	0005524	molecular_function	ATP binding
E	0006259	biological_process	DNA metabolic process
E	0006265	biological_process	DNA topological change
F	0003677	molecular_function	DNA binding
F	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
F	0005524	molecular_function	ATP binding
F	0006259	biological_process	DNA metabolic process
F	0006265	biological_process	DNA topological change

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 601

Chain	Residue
A	TYR321
A	LYS322
A	THR324
A	GLN327

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 601

Chain	Residue
B	TYR321
B	LYS322
B	THR324
B	GLN327

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K C 601

Chain	Residue
C	LYS322
C	THR324
C	GLN327
C	TYR321

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K D 601

Chain	Residue
D	TYR321
D	LYS322
D	THR324
D	GLN327

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K E 601

Chain	Residue
E	TYR321
E	LYS322
E	THR324
E	GLN327

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K F 601

Chain	Residue
F	TYR321
F	LYS322
F	THR324
F	GLN327

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE TRS F 602

Chain	Residue
F	ASP96

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|HAMAP-Rule:MF_01897

Chain	Residue	Details
A	TYR123
B	TYR123
C	TYR123
D	TYR123
E	TYR123
F	TYR123

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