Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XGZ

Crystal structure of E. coli MlaFB ABC transport subunits in the monomeric state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0015914	biological_process	phospholipid transport
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0120010	biological_process	intermembrane phospholipid transfer
A	0120014	molecular_function	phospholipid transfer activity
A	1990531	cellular_component	phospholipid-translocating ATPase complex
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006974	biological_process	DNA damage response
B	0015914	biological_process	phospholipid transport
B	0016020	cellular_component	membrane
B	0046677	biological_process	response to antibiotic
B	0120010	biological_process	intermembrane phospholipid transfer
B	0120014	molecular_function	phospholipid transfer activity
B	1990531	cellular_component	phospholipid-translocating ATPase complex
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005886	cellular_component	plasma membrane
C	0015914	biological_process	phospholipid transport
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0120010	biological_process	intermembrane phospholipid transfer
C	0120014	molecular_function	phospholipid transfer activity
C	1990531	cellular_component	phospholipid-translocating ATPase complex
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006974	biological_process	DNA damage response
D	0015914	biological_process	phospholipid transport
D	0016020	cellular_component	membrane
D	0046677	biological_process	response to antibiotic
D	0120010	biological_process	intermembrane phospholipid transfer
D	0120014	molecular_function	phospholipid transfer activity
D	1990531	cellular_component	phospholipid-translocating ATPase complex
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005886	cellular_component	plasma membrane
E	0015914	biological_process	phospholipid transport
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0120010	biological_process	intermembrane phospholipid transfer
E	0120014	molecular_function	phospholipid transfer activity
E	1990531	cellular_component	phospholipid-translocating ATPase complex
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006974	biological_process	DNA damage response
F	0015914	biological_process	phospholipid transport
F	0016020	cellular_component	membrane
F	0046677	biological_process	response to antibiotic
F	0120010	biological_process	intermembrane phospholipid transfer
F	0120014	molecular_function	phospholipid transfer activity
F	1990531	cellular_component	phospholipid-translocating ATPase complex
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005886	cellular_component	plasma membrane
G	0015914	biological_process	phospholipid transport
G	0016020	cellular_component	membrane
G	0016887	molecular_function	ATP hydrolysis activity
G	0120010	biological_process	intermembrane phospholipid transfer
G	0120014	molecular_function	phospholipid transfer activity
G	1990531	cellular_component	phospholipid-translocating ATPase complex
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006974	biological_process	DNA damage response
H	0015914	biological_process	phospholipid transport
H	0016020	cellular_component	membrane
H	0046677	biological_process	response to antibiotic
H	0120010	biological_process	intermembrane phospholipid transfer
H	0120014	molecular_function	phospholipid transfer activity
H	1990531	cellular_component	phospholipid-translocating ATPase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue PO4 A 301

Chain	Residue
A	GLY44
A	ILE45
A	GLY46
A	LYS47
A	THR48
A	PO4302
A	EDO304

site_id	AC2
Number of Residues	5
Details	binding site for residue PO4 A 302

Chain	Residue
A	GLU170
A	HIS203
A	PO4301
A	SER43
A	LYS47

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 303

Chain	Residue
A	GLY259
A	ASP264
C	ARG135
C	LYS139

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 304

Chain	Residue
A	THR49
A	ARG52
A	PO4301

site_id	AC5
Number of Residues	7
Details	binding site for residue PO4 C 301

Chain	Residue
C	SER43
C	GLY44
C	ILE45
C	GLY46
C	LYS47
C	THR48
C	PO4302

site_id	AC6
Number of Residues	5
Details	binding site for residue PO4 C 302

Chain	Residue
C	SER43
C	LYS47
C	GLU170
C	HIS203
C	PO4301

site_id	AC7
Number of Residues	8
Details	binding site for residue GOL C 303

Chain	Residue
A	GLN230
A	TYR256
A	ALA258
C	GLU130
C	GLY133
C	LEU134
C	ARG135
C	GLY136

site_id	AC8
Number of Residues	7
Details	binding site for residue PO4 E 301

Chain	Residue
E	SER43
E	GLY44
E	ILE45
E	GLY46
E	LYS47
E	THR48
E	PO4302

site_id	AC9
Number of Residues	5
Details	binding site for residue PO4 E 302

Chain	Residue
E	SER43
E	LYS47
E	GLU170
E	HIS203
E	PO4301

site_id	AD1
Number of Residues	2
Details	binding site for residue GOL E 303

Chain	Residue
E	GLU207
G	GLU207

site_id	AD2
Number of Residues	5
Details	binding site for residue PO4 G 301

Chain	Residue
G	SER43
G	LYS47
G	GLU170
G	HIS203
G	PO4302

site_id	AD3
Number of Residues	7
Details	binding site for residue PO4 G 302

Chain	Residue
G	SER43
G	GLY44
G	ILE45
G	GLY46
G	LYS47
G	THR48
G	PO4301

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU145-ILE159

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00434

Chain	Residue	Details
A	GLY41
C	GLY41
E	GLY41
G	GLY41

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)