7VGF

cryo-EM structure of AMP-PNP bound human ABCB7

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	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006783	biological_process	heme biosynthetic process
A	0006879	biological_process	intracellular iron ion homeostasis
A	0015232	molecular_function	heme transmembrane transporter activity
A	0015886	biological_process	heme transport
A	0016020	cellular_component	membrane
A	0016226	biological_process	iron-sulfur cluster assembly
A	0016887	molecular_function	ATP hydrolysis activity
A	0031966	cellular_component	mitochondrial membrane
A	0034755	biological_process	iron ion transmembrane 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	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
A	0055085	biological_process	transmembrane transport
A	0070455	biological_process	positive regulation of heme biosynthetic process
A	0140359	molecular_function	ABC-type transporter activity
A	0140466	biological_process	iron-sulfur cluster export from the mitochondrion
A	0140481	molecular_function	ABC-type iron-sulfur cluster transporter activity
A	1903331	biological_process	positive regulation of iron-sulfur cluster assembly
A	1903427	biological_process	negative regulation of reactive oxygen species biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006783	biological_process	heme biosynthetic process
B	0006879	biological_process	intracellular iron ion homeostasis
B	0015232	molecular_function	heme transmembrane transporter activity
B	0015886	biological_process	heme transport
B	0016020	cellular_component	membrane
B	0016226	biological_process	iron-sulfur cluster assembly
B	0016887	molecular_function	ATP hydrolysis activity
B	0031966	cellular_component	mitochondrial membrane
B	0034755	biological_process	iron ion transmembrane 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	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
B	0055085	biological_process	transmembrane transport
B	0070455	biological_process	positive regulation of heme biosynthetic process
B	0140359	molecular_function	ABC-type transporter activity
B	0140466	biological_process	iron-sulfur cluster export from the mitochondrion
B	0140481	molecular_function	ABC-type iron-sulfur cluster transporter activity
B	1903331	biological_process	positive regulation of iron-sulfur cluster assembly
B	1903427	biological_process	negative regulation of reactive oxygen species biosynthetic process

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU609-ILE623

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	240
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	244
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q2G506","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9NP58","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q704E8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q704E8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q704E8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---