2NUU

Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0008519	molecular_function	ammonium channel activity
A	0015670	biological_process	carbon dioxide transport
A	0016020	cellular_component	membrane
A	0042802	molecular_function	identical protein binding
A	0072488	biological_process	ammonium transmembrane transport
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
B	0008519	molecular_function	ammonium channel activity
B	0015670	biological_process	carbon dioxide transport
B	0016020	cellular_component	membrane
B	0042802	molecular_function	identical protein binding
B	0072488	biological_process	ammonium transmembrane transport
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
C	0008519	molecular_function	ammonium channel activity
C	0015670	biological_process	carbon dioxide transport
C	0016020	cellular_component	membrane
C	0042802	molecular_function	identical protein binding
C	0072488	biological_process	ammonium transmembrane transport
D	0005515	molecular_function	protein binding
D	0005886	cellular_component	plasma membrane
D	0008519	molecular_function	ammonium channel activity
D	0015670	biological_process	carbon dioxide transport
D	0016020	cellular_component	membrane
D	0042802	molecular_function	identical protein binding
D	0072488	biological_process	ammonium transmembrane transport
E	0005515	molecular_function	protein binding
E	0005886	cellular_component	plasma membrane
E	0008519	molecular_function	ammonium channel activity
E	0015670	biological_process	carbon dioxide transport
E	0016020	cellular_component	membrane
E	0042802	molecular_function	identical protein binding
E	0072488	biological_process	ammonium transmembrane transport
F	0005515	molecular_function	protein binding
F	0005886	cellular_component	plasma membrane
F	0008519	molecular_function	ammonium channel activity
F	0015670	biological_process	carbon dioxide transport
F	0016020	cellular_component	membrane
F	0042802	molecular_function	identical protein binding
F	0072488	biological_process	ammonium transmembrane transport
G	0000166	molecular_function	nucleotide binding
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0005886	cellular_component	plasma membrane
G	0006808	biological_process	regulation of nitrogen utilization
G	0030234	molecular_function	enzyme regulator activity
G	0042802	molecular_function	identical protein binding
G	0045848	biological_process	positive regulation of nitrogen utilization
H	0000166	molecular_function	nucleotide binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005886	cellular_component	plasma membrane
H	0006808	biological_process	regulation of nitrogen utilization
H	0030234	molecular_function	enzyme regulator activity
H	0042802	molecular_function	identical protein binding
H	0045848	biological_process	positive regulation of nitrogen utilization
I	0000166	molecular_function	nucleotide binding
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0005886	cellular_component	plasma membrane
I	0006808	biological_process	regulation of nitrogen utilization
I	0030234	molecular_function	enzyme regulator activity
I	0042802	molecular_function	identical protein binding
I	0045848	biological_process	positive regulation of nitrogen utilization
J	0000166	molecular_function	nucleotide binding
J	0005515	molecular_function	protein binding
J	0005524	molecular_function	ATP binding
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0005886	cellular_component	plasma membrane
J	0006808	biological_process	regulation of nitrogen utilization
J	0030234	molecular_function	enzyme regulator activity
J	0042802	molecular_function	identical protein binding
J	0045848	biological_process	positive regulation of nitrogen utilization
K	0000166	molecular_function	nucleotide binding
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0005886	cellular_component	plasma membrane
K	0006808	biological_process	regulation of nitrogen utilization
K	0030234	molecular_function	enzyme regulator activity
K	0042802	molecular_function	identical protein binding
K	0045848	biological_process	positive regulation of nitrogen utilization
L	0000166	molecular_function	nucleotide binding
L	0005515	molecular_function	protein binding
L	0005524	molecular_function	ATP binding
L	0005737	cellular_component	cytoplasm
L	0005829	cellular_component	cytosol
L	0005886	cellular_component	plasma membrane
L	0006808	biological_process	regulation of nitrogen utilization
L	0030234	molecular_function	enzyme regulator activity
L	0042802	molecular_function	identical protein binding
L	0045848	biological_process	positive regulation of nitrogen utilization

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ADP G 1200

Chain	Residue
G	GLY27
H	GLY35
H	PHE36
H	ARG38
H	GLN39
H	LYS58
H	GLY87
H	ASP88
H	GLY89
H	LYS90
H	HOH1308
G	LEU28
G	THR29
G	ASP62
G	VAL63
G	ALA64
G	ARG101
G	ARG103
G	HOH1411

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP H 1300

Chain	Residue
H	GLY27
H	LEU28
H	THR29
H	ASP62
H	VAL63
H	ALA64
H	ARG101
H	ARG103
H	HOH1315
I	GLY35
I	PHE36
I	GLY37
I	ARG38
I	GLN39
I	GLY87
I	LYS90

---

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP G 1400

Chain	Residue
G	ILE7
G	GLY35
G	PHE36
G	ARG38
G	GLN39
G	LYS58
G	GLY87
G	ASP88
G	GLY89
G	LYS90
G	HOH1403
G	HOH1407
I	GLY27
I	LEU28
I	THR29
I	ASP62
I	VAL63
I	ALA64
I	ARG101
I	ARG103

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP J 1500

Chain	Residue
J	GLY27
J	LEU28
J	THR29
J	ASP62
J	VAL63
J	ALA64
J	ARG101
J	ARG103
J	LEU112
J	HOH1707
K	ILE7
K	GLY35
K	PHE36
K	ARG38
K	GLN39
K	LYS58
K	GLY87
K	ASP88
K	GLY89
K	LYS90
K	HOH121

---

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP L 1600

Chain	Residue
K	GLY27
K	LEU28
K	THR29
K	ASP62
K	VAL63
K	ALA64
K	ARG101
K	ARG103
L	ILE7
L	GLY35
L	PHE36
L	GLY37
L	ARG38
L	GLN39
L	LYS58
L	GLY87
L	ASP88
L	GLY89
L	LYS90
L	PHE92
L	HOH1610

---

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ADP J 1700

Chain	Residue
J	GLY37
J	ARG38
J	GLN39
J	LYS58
J	GLY87
J	ASP88
J	GLY89
J	LYS90
J	HOH1712
J	HOH1714
L	GLY27
L	LEU28
L	THR29
L	ASP62
L	VAL63
L	ALA64
L	ARG101
L	ARG103
J	GLY35
J	PHE36

---

Functional Information from PROSITE/UniProt

site_id	PS00496
Number of Residues	6
Details	PII_GLNB_UMP P-II protein uridylation site. YRGAEY

Chain	Residue	Details
G	TYR46-TYR51

---

site_id	PS00638
Number of Residues	14
Details	PII_GLNB_CTER P-II protein C-terminal region signature. TgkiGDGKIFVaeL

Chain	Residue	Details
G	THR83-LEU96

---

site_id	PS01219
Number of Residues	26
Details	AMMONIUM_TRANSP Ammonium transporters signature. DFAGGtvVhinAAiaGLvgaYLiGkR

Chain	Residue	Details
A	ASP160-ARG185

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1416
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"15361618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15563598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17040913","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	288
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15361618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15563598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17040913","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	372
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15361618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15563598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17040913","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	168
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15361618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15563598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17040913","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15361618","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Site: {"description":"Important for the deprotonation of the ammonium cation","evidences":[{"source":"PubMed","id":"19278252","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	12
Details	Site: {"description":"Twin-His motif. Important for optimum substrate conductance","evidences":[{"source":"PubMed","id":"17040913","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23667517","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32662768","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Site: {"description":"Important for optimum substrate conductance","evidences":[{"source":"PubMed","id":"18362341","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17220269","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NUU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9733647","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GNK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17190799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17220269","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NS1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NUU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	6
Details	Modified residue: {"description":"O-UMP-tyrosine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00675","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---