Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6R72

Crystal structure of BmrA-E504A in an outward-facing conformation

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	0006869	biological_process	lipid transport
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0034040	molecular_function	ATPase-coupled lipid transmembrane transporter activity
A	0046677	biological_process	response to antibiotic
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	0006869	biological_process	lipid transport
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0034040	molecular_function	ATPase-coupled lipid transmembrane transporter activity
B	0046677	biological_process	response to antibiotic
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	0006869	biological_process	lipid transport
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0034040	molecular_function	ATPase-coupled lipid transmembrane transporter activity
C	0046677	biological_process	response to antibiotic
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	0006869	biological_process	lipid transport
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0034040	molecular_function	ATPase-coupled lipid transmembrane transporter activity
D	0046677	biological_process	response to antibiotic
D	0055085	biological_process	transmembrane transport
D	0140359	molecular_function	ABC-type transporter activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue ATP A 700

Chain	Residue
A	ASP116
A	THR381
A	THR382
A	LYS385
A	GLN422
A	MG701
B	LEU464
B	ILE477
B	MET478
B	SER480
B	GLY481
A	TYR350
B	GLY482
B	GLN483
A	ILE356
A	PRO375
A	SER376
A	GLY377
A	GLY378
A	GLY379
A	LYS380

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 701

Chain	Residue
A	THR381
A	GLN422
A	ATP700

site_id	AC3
Number of Residues	18
Details	binding site for residue ATP B 700

Chain	Residue
A	ILE477
A	MET478
A	SER480
A	GLY481
A	GLY482
A	GLN483
B	ASP116
B	TYR350
B	SER376
B	GLY377
B	GLY378
B	GLY379
B	LYS380
B	THR381
B	THR382
B	LYS385
B	GLN422
B	MG701

site_id	AC4
Number of Residues	3
Details	binding site for residue MG B 701

Chain	Residue
B	THR381
B	GLN422
B	ATP700

site_id	AC5
Number of Residues	20
Details	binding site for residue ATP C 700

Chain	Residue
C	ASP116
C	TYR350
C	ILE356
C	SER376
C	GLY377
C	GLY378
C	GLY379
C	LYS380
C	THR381
C	THR382
C	LYS385
C	GLN422
C	MG701
D	LEU464
D	ILE477
D	MET478
D	SER480
D	GLY481
D	GLY482
D	GLN483

site_id	AC6
Number of Residues	4
Details	binding site for residue MG C 701

Chain	Residue
C	THR381
C	GLN422
C	ASP503
C	ATP700

site_id	AC7
Number of Residues	20
Details	binding site for residue ATP D 700

Chain	Residue
C	GLU463
C	LEU464
C	ILE477
C	MET478
C	SER480
C	GLY481
C	GLY482
C	GLN483
D	ASP116
D	TYR350
D	SER376
D	GLY377
D	GLY378
D	GLY379
D	LYS380
D	THR381
D	THR382
D	LYS385
D	GLN422
D	MG701

site_id	AC8
Number of Residues	4
Details	binding site for residue MG D 701

Chain	Residue
D	THR381
D	GLN422
D	ASP503
D	ATP700

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU479-LEU493

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	380
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	940
Details	Domain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details