5IUL

Crystal structure of the DesK-DesR complex in the phosphotransfer state with high Mg2+ (150 mM) and BeF3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000155	molecular_function	phosphorelay sensor kinase activity
A	0000160	biological_process	phosphorelay signal transduction system
A	0016020	cellular_component	membrane
A	0046983	molecular_function	protein dimerization activity
B	0000155	molecular_function	phosphorelay sensor kinase activity
B	0000160	biological_process	phosphorelay signal transduction system
B	0016020	cellular_component	membrane
B	0046983	molecular_function	protein dimerization activity
C	0000160	biological_process	phosphorelay signal transduction system
D	0000155	molecular_function	phosphorelay sensor kinase activity
D	0000160	biological_process	phosphorelay signal transduction system
D	0016020	cellular_component	membrane
D	0046983	molecular_function	protein dimerization activity
E	0000155	molecular_function	phosphorelay sensor kinase activity
E	0000160	biological_process	phosphorelay signal transduction system
E	0016020	cellular_component	membrane
E	0046983	molecular_function	protein dimerization activity
F	0000160	biological_process	phosphorelay signal transduction system

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue ACP A 401

Chain	Residue
A	GLU289
A	GLY326
A	HIS335
A	GLY336
A	LEU337
A	THR359
A	MG402
A	HOH502
A	HOH503
A	ASN293
A	LYS296
A	HIS297
A	SER298
A	ASP320
A	THR323
A	PHE324
A	LYS325

---

site_id	AC2
Number of Residues	4
Details	binding site for residue MG A 402

Chain	Residue
A	GLU289
A	ASN293
A	ACP401
A	HOH502

---

site_id	AC3
Number of Residues	17
Details	binding site for residue ACP B 401

Chain	Residue
B	GLU289
B	ASN293
B	LYS296
B	HIS297
B	SER298
B	ASP320
B	THR323
B	PHE324
B	LYS325
B	GLY326
B	HIS335
B	GLY336
B	LEU337
B	THR359
B	MG402
B	HOH501
D	LYS312

---

site_id	AC4
Number of Residues	4
Details	binding site for residue MG B 402

Chain	Residue
B	GLU289
B	ASN293
B	ACP401
B	HOH501

---

site_id	AC5
Number of Residues	6
Details	binding site for residue MG C 201

Chain	Residue
C	ASP9
C	ASP54
C	GLU56
C	HOH302
C	HOH304
C	HOH306

---

site_id	AC6
Number of Residues	3
Details	binding site for residue K C 202

Chain	Residue
C	ASN22
C	GLU24
C	MET27

---

site_id	AC7
Number of Residues	3
Details	binding site for residue K C 203

Chain	Residue
C	LEU69
C	LYS70
C	THR72

---

site_id	AC8
Number of Residues	17
Details	binding site for residue ACP D 401

Chain	Residue
D	GLU289
D	ASN293
D	LYS296
D	HIS297
D	SER298
D	ASP320
D	THR323
D	PHE324
D	LYS325
D	GLY326
D	HIS335
D	GLY336
D	LEU337
D	THR359
D	MG402
D	HOH501
D	HOH502

---

site_id	AC9
Number of Residues	4
Details	binding site for residue MG D 402

Chain	Residue
D	GLU289
D	ASN293
D	ACP401
D	HOH501

---

site_id	AD1
Number of Residues	17
Details	binding site for residue ACP E 401

Chain	Residue
A	LYS312
E	GLU289
E	ASN293
E	LYS296
E	HIS297
E	SER298
E	ASP320
E	THR323
E	PHE324
E	LYS325
E	GLY326
E	HIS335
E	GLY336
E	LEU337
E	THR359
E	MG402
E	HOH501

---

site_id	AD2
Number of Residues	4
Details	binding site for residue MG E 402

Chain	Residue
E	GLU289
E	ASN293
E	ACP401
E	HOH501

---

site_id	AD3
Number of Residues	6
Details	binding site for residue MG F 201

Chain	Residue
F	HOH302
F	HOH303
F	HOH304
F	ASP9
F	ASP54
F	GLU56

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Modified residue: {"description":"Phosphohistidine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	228
Details	Domain: {"description":"Response regulatory","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00169","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---