Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6HZM

Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005654	cellular_component	nucleoplasm
A	0005739	cellular_component	mitochondrion
A	0005886	cellular_component	plasma membrane
A	0006869	biological_process	lipid transport
A	0008514	molecular_function	organic anion transmembrane transporter activity
A	0008559	molecular_function	ABC-type xenobiotic transporter activity
A	0015143	molecular_function	urate transmembrane transporter activity
A	0015225	molecular_function	biotin transmembrane transporter activity
A	0015562	molecular_function	efflux transmembrane transporter activity
A	0015711	biological_process	organic anion transport
A	0015747	biological_process	urate transport
A	0015878	biological_process	biotin transport
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0030148	biological_process	sphingolipid biosynthetic process
A	0031526	cellular_component	brush border membrane
A	0031966	cellular_component	mitochondrial membrane
A	0032217	molecular_function	riboflavin transmembrane transporter activity
A	0032218	biological_process	riboflavin transport
A	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0042910	molecular_function	xenobiotic transmembrane transporter activity
A	0045121	cellular_component	membrane raft
A	0046415	biological_process	urate metabolic process
A	0046624	molecular_function	sphingolipid transporter activity
A	0046983	molecular_function	protein dimerization activity
A	0055085	biological_process	transmembrane transport
A	0070633	biological_process	transepithelial transport
A	0097744	biological_process	renal urate salt excretion
A	0098591	cellular_component	external side of apical plasma membrane
A	0140115	biological_process	export across plasma membrane
A	0140359	molecular_function	ABC-type transporter activity
A	0150104	biological_process	transport across blood-brain barrier
A	1990748	biological_process	cellular detoxification
A	1990962	biological_process	xenobiotic transport across blood-brain barrier
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005654	cellular_component	nucleoplasm
B	0005739	cellular_component	mitochondrion
B	0005886	cellular_component	plasma membrane
B	0006869	biological_process	lipid transport
B	0008514	molecular_function	organic anion transmembrane transporter activity
B	0008559	molecular_function	ABC-type xenobiotic transporter activity
B	0015143	molecular_function	urate transmembrane transporter activity
B	0015225	molecular_function	biotin transmembrane transporter activity
B	0015562	molecular_function	efflux transmembrane transporter activity
B	0015711	biological_process	organic anion transport
B	0015747	biological_process	urate transport
B	0015878	biological_process	biotin transport
B	0016020	cellular_component	membrane
B	0016324	cellular_component	apical plasma membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0030148	biological_process	sphingolipid biosynthetic process
B	0031526	cellular_component	brush border membrane
B	0031966	cellular_component	mitochondrial membrane
B	0032217	molecular_function	riboflavin transmembrane transporter activity
B	0032218	biological_process	riboflavin transport
B	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0042910	molecular_function	xenobiotic transmembrane transporter activity
B	0045121	cellular_component	membrane raft
B	0046415	biological_process	urate metabolic process
B	0046624	molecular_function	sphingolipid transporter activity
B	0046983	molecular_function	protein dimerization activity
B	0055085	biological_process	transmembrane transport
B	0070633	biological_process	transepithelial transport
B	0097744	biological_process	renal urate salt excretion
B	0098591	cellular_component	external side of apical plasma membrane
B	0140115	biological_process	export across plasma membrane
B	0140359	molecular_function	ABC-type transporter activity
B	0150104	biological_process	transport across blood-brain barrier
B	1990748	biological_process	cellular detoxification
B	1990962	biological_process	xenobiotic transport across blood-brain barrier

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue ATP A 1501

Chain	Residue
A	VAL46
A	SER87
A	SER88
A	GLN126
A	GLN211
A	HIS243
A	MG1502
A	HOH1602
B	LYS172
B	ARG184
B	GLY185
A	LEU48
B	SER187
B	GLY188
B	GLY189
B	GLU190
A	LYS61
A	ILE63
A	THR82
A	GLY83
A	GLY84
A	GLY85
A	LYS86

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 1502

Chain	Residue
A	SER87
A	GLN126
A	GLN211
A	ATP1501
A	HOH1602

site_id	AC3
Number of Residues	23
Details	binding site for residue ATP B 1501

Chain	Residue
A	LYS172
A	ARG184
A	GLY185
A	SER187
A	GLY188
A	GLY189
A	GLU190
B	VAL46
B	LEU48
B	LYS61
B	ILE63
B	THR82
B	GLY83
B	GLY84
B	GLY85
B	LYS86
B	SER87
B	SER88
B	GLN126
B	GLN211
B	HIS243
B	MG1502
B	HOH1602

site_id	AC4
Number of Residues	5
Details	binding site for residue MG B 1502

Chain	Residue
B	SER87
B	GLN126
B	GLN211
B	ATP1501
B	HOH1602

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	240
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	182
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	68
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	524
Details	Domain: {"description":"ABC transmembrane type-2"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30405239","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HZM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30405239","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HZM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"15807535","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15807535","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28554189","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NJ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NJG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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