1F51

A TRANSIENT INTERACTION BETWEEN TWO PHOSPHORELAY PROTEINS TRAPPED IN A CRYSTAL LATTICE REVEALS THE MECHANISM OF MOLECULAR RECOGNITION AND PHOSPHOTRANSFER IN SINGAL TRANSDUCTION

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	0005737	cellular_component	cytoplasm
A	0016301	molecular_function	kinase activity
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0030435	biological_process	sporulation resulting in formation of a cellular spore
B	0000155	molecular_function	phosphorelay sensor kinase activity
B	0000160	biological_process	phosphorelay signal transduction system
B	0005737	cellular_component	cytoplasm
B	0016301	molecular_function	kinase activity
B	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
B	0030435	biological_process	sporulation resulting in formation of a cellular spore
C	0000155	molecular_function	phosphorelay sensor kinase activity
C	0000160	biological_process	phosphorelay signal transduction system
C	0005737	cellular_component	cytoplasm
C	0016301	molecular_function	kinase activity
C	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
C	0030435	biological_process	sporulation resulting in formation of a cellular spore
D	0000155	molecular_function	phosphorelay sensor kinase activity
D	0000160	biological_process	phosphorelay signal transduction system
D	0005737	cellular_component	cytoplasm
D	0016301	molecular_function	kinase activity
D	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
D	0030435	biological_process	sporulation resulting in formation of a cellular spore
E	0000160	biological_process	phosphorelay signal transduction system
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0016301	molecular_function	kinase activity
E	0030435	biological_process	sporulation resulting in formation of a cellular spore
E	0046872	molecular_function	metal ion binding
F	0000160	biological_process	phosphorelay signal transduction system
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0016301	molecular_function	kinase activity
F	0030435	biological_process	sporulation resulting in formation of a cellular spore
F	0046872	molecular_function	metal ion binding
G	0000160	biological_process	phosphorelay signal transduction system
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0016301	molecular_function	kinase activity
G	0030435	biological_process	sporulation resulting in formation of a cellular spore
G	0046872	molecular_function	metal ion binding
H	0000160	biological_process	phosphorelay signal transduction system
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0016301	molecular_function	kinase activity
H	0030435	biological_process	sporulation resulting in formation of a cellular spore
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 2001

Chain	Residue
E	ASP1211
E	GLN1212
E	ASP1254
E	LYS1256

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG F 2002

Chain	Residue
F	ASP1011
F	ASP1054

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG H 2003

Chain	Residue
H	LYS1456
D	HIS630
H	ASP1411
H	ASP1454

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: Phosphohistidine => ECO:0000269|PubMed:9726997

Chain	Residue	Details
A	HIS30
G	ASP1611
G	ASP1654
G	LYS1656
H	ASP1410
H	ASP1411
H	ASP1454
H	LYS1456
B	HIS230
C	HIS430
D	HIS630
F	ASP1010
F	ASP1011
F	ASP1054
F	LYS1056
G	ASP1610

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site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:9254596

Chain	Residue	Details
E	ASP1254
F	ASP1054
G	ASP1654
H	ASP1454

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