6PAR

Structure of a bacterial Atm1-family ABC exporter with MgAMPPNP bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
A	0046689	biological_process	response to mercury ion
A	0055085	biological_process	transmembrane transport
A	0140359	molecular_function	ABC-type transporter activity
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005886	cellular_component	plasma membrane
B	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
B	0046689	biological_process	response to mercury ion
B	0055085	biological_process	transmembrane transport
B	0140359	molecular_function	ABC-type transporter activity
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0005886	cellular_component	plasma membrane
C	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
C	0046689	biological_process	response to mercury ion
C	0055085	biological_process	transmembrane transport
C	0140359	molecular_function	ABC-type transporter activity
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0005886	cellular_component	plasma membrane
D	0006811	biological_process	monoatomic ion transport
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
D	0046689	biological_process	response to mercury ion
D	0055085	biological_process	transmembrane transport
D	0140359	molecular_function	ABC-type transporter activity
E	0000166	molecular_function	nucleotide binding
E	0005524	molecular_function	ATP binding
E	0005886	cellular_component	plasma membrane
E	0006811	biological_process	monoatomic ion transport
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
E	0046689	biological_process	response to mercury ion
E	0055085	biological_process	transmembrane transport
E	0140359	molecular_function	ABC-type transporter activity
F	0000166	molecular_function	nucleotide binding
F	0005524	molecular_function	ATP binding
F	0005886	cellular_component	plasma membrane
F	0006811	biological_process	monoatomic ion transport
F	0016020	cellular_component	membrane
F	0016887	molecular_function	ATP hydrolysis activity
F	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
F	0046689	biological_process	response to mercury ion
F	0055085	biological_process	transmembrane transport
F	0140359	molecular_function	ABC-type transporter activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue ANP A 701

Chain	Residue
A	TYR370
A	SER401
A	THR402
A	GLN442
A	HIS554
A	MG702
B	PHE479
B	LYS497
B	SER499
B	GLY500
B	GLY501
A	ARG374
B	GLU502
A	ILE376
A	PRO395
A	SER396
A	GLY397
A	ALA398
A	GLY399
A	LYS400

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 702

Chain	Residue
A	SER401
A	GLN442
A	ANP701

---

site_id	AC3
Number of Residues	21
Details	binding site for residue ANP B 701

Chain	Residue
A	PHE479
A	LYS497
A	SER499
A	GLY500
A	GLY501
A	GLU502
A	ALA527
B	TYR370
B	ARG374
B	ILE376
B	SER396
B	GLY397
B	ALA398
B	GLY399
B	LYS400
B	SER401
B	THR402
B	TYR411
B	GLN442
B	HIS554
B	MG702

---

site_id	AC4
Number of Residues	3
Details	binding site for residue MG B 702

Chain	Residue
B	SER401
B	GLN442
B	ANP701

---

site_id	AC5
Number of Residues	18
Details	binding site for residue ANP C 701

Chain	Residue
C	TYR370
C	ARG374
C	PRO395
C	SER396
C	GLY397
C	ALA398
C	GLY399
C	LYS400
C	SER401
C	THR402
C	GLN442
C	MG702
D	LYS497
D	SER499
D	GLY500
D	GLY501
D	GLU502
D	ALA527

---

site_id	AC6
Number of Residues	4
Details	binding site for residue MG C 702

Chain	Residue
C	SER401
C	GLN442
C	ASP522
C	ANP701

---

site_id	AC7
Number of Residues	18
Details	binding site for residue ANP D 701

Chain	Residue
C	LYS497
C	SER499
C	GLY500
C	GLU502
C	ALA527
D	TYR370
D	ARG374
D	ILE376
D	SER396
D	GLY397
D	ALA398
D	GLY399
D	LYS400
D	SER401
D	THR402
D	GLN442
D	HIS554
D	MG702

---

site_id	AC8
Number of Residues	3
Details	binding site for residue MG D 702

Chain	Residue
D	SER401
D	GLN442
D	ANP701

---

site_id	AC9
Number of Residues	19
Details	binding site for residue ANP E 701

Chain	Residue
E	THR402
E	GLN442
E	HIS554
E	MG702
F	PHE479
F	LYS497
F	SER499
F	GLY500
F	GLY501
F	GLU502
E	TYR370
E	ARG374
E	PRO395
E	SER396
E	GLY397
E	ALA398
E	GLY399
E	LYS400
E	SER401

---

site_id	AD1
Number of Residues	3
Details	binding site for residue MG E 702

Chain	Residue
E	SER401
E	GLN442
E	ANP701

---

site_id	AD2
Number of Residues	20
Details	binding site for residue ANP F 701

Chain	Residue
E	PHE479
E	LYS497
E	SER499
E	GLY500
E	GLY501
E	GLU502
E	ALA527
F	TYR370
F	ARG374
F	PRO395
F	SER396
F	GLY397
F	ALA398
F	GLY399
F	LYS400
F	SER401
F	THR402
F	GLN442
F	HIS554
F	MG702

---

site_id	AD3
Number of Residues	3
Details	binding site for residue MG F 702

Chain	Residue
F	SER401
F	GLN442
F	ANP701

---

Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKQRVAIARTL

Chain	Residue	Details
A	LEU498-LEU512

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	762
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	216
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	666
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1728
Details	Domain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1404
Details	Domain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MRP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9NP58","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	66
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---