Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7NY1

Structure of the fungal plasma membrane proton pump Pma1 in its auto-inhibited state - hexameric assembly

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005215	molecular_function	transporter activity
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0008553	molecular_function	P-type proton-exporting transporter activity
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0046872	molecular_function	metal ion binding
A	0051453	biological_process	regulation of intracellular pH
A	0120029	biological_process	proton export across plasma membrane
A	1902600	biological_process	proton transmembrane transport
B	0000166	molecular_function	nucleotide binding
B	0005215	molecular_function	transporter activity
B	0005524	molecular_function	ATP binding
B	0005886	cellular_component	plasma membrane
B	0006811	biological_process	monoatomic ion transport
B	0008553	molecular_function	P-type proton-exporting transporter activity
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0046872	molecular_function	metal ion binding
B	0051453	biological_process	regulation of intracellular pH
B	0120029	biological_process	proton export across plasma membrane
B	1902600	biological_process	proton transmembrane transport
C	0000166	molecular_function	nucleotide binding
C	0005215	molecular_function	transporter activity
C	0005524	molecular_function	ATP binding
C	0005886	cellular_component	plasma membrane
C	0006811	biological_process	monoatomic ion transport
C	0008553	molecular_function	P-type proton-exporting transporter activity
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0046872	molecular_function	metal ion binding
C	0051453	biological_process	regulation of intracellular pH
C	0120029	biological_process	proton export across plasma membrane
C	1902600	biological_process	proton transmembrane transport
D	0000166	molecular_function	nucleotide binding
D	0005215	molecular_function	transporter activity
D	0005524	molecular_function	ATP binding
D	0005886	cellular_component	plasma membrane
D	0006811	biological_process	monoatomic ion transport
D	0008553	molecular_function	P-type proton-exporting transporter activity
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0046872	molecular_function	metal ion binding
D	0051453	biological_process	regulation of intracellular pH
D	0120029	biological_process	proton export across plasma membrane
D	1902600	biological_process	proton transmembrane transport
E	0000166	molecular_function	nucleotide binding
E	0005215	molecular_function	transporter activity
E	0005524	molecular_function	ATP binding
E	0005886	cellular_component	plasma membrane
E	0006811	biological_process	monoatomic ion transport
E	0008553	molecular_function	P-type proton-exporting transporter activity
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0046872	molecular_function	metal ion binding
E	0051453	biological_process	regulation of intracellular pH
E	0120029	biological_process	proton export across plasma membrane
E	1902600	biological_process	proton transmembrane transport
F	0000166	molecular_function	nucleotide binding
F	0005215	molecular_function	transporter activity
F	0005524	molecular_function	ATP binding
F	0005886	cellular_component	plasma membrane
F	0006811	biological_process	monoatomic ion transport
F	0008553	molecular_function	P-type proton-exporting transporter activity
F	0016020	cellular_component	membrane
F	0016887	molecular_function	ATP hydrolysis activity
F	0046872	molecular_function	metal ion binding
F	0051453	biological_process	regulation of intracellular pH
F	0120029	biological_process	proton export across plasma membrane
F	1902600	biological_process	proton transmembrane transport

Functional Information from PROSITE/UniProt

site_id	PS00154
Number of Residues	7
Details	ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT

Chain	Residue	Details
A	ASP378-THR384

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	132
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	264
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	114
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	132
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	192
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2082
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	150
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	102
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	144
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	114
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	120
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	144
Details	Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	6
Details	Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)