Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5OCH

The crystal structure of human ABCB8 in an outward-facing state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0055085	biological_process	transmembrane transport
A	0140359	molecular_function	ABC-type transporter activity
B	0005524	molecular_function	ATP binding
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0055085	biological_process	transmembrane transport
B	0140359	molecular_function	ABC-type transporter activity
C	0005524	molecular_function	ATP binding
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0055085	biological_process	transmembrane transport
C	0140359	molecular_function	ABC-type transporter activity
D	0005524	molecular_function	ATP binding
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0055085	biological_process	transmembrane transport
D	0140359	molecular_function	ABC-type transporter activity
E	0005524	molecular_function	ATP binding
E	0016020	cellular_component	membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0055085	biological_process	transmembrane transport
E	0140359	molecular_function	ABC-type transporter activity
F	0005524	molecular_function	ATP binding
F	0016020	cellular_component	membrane
F	0016887	molecular_function	ATP hydrolysis activity
F	0055085	biological_process	transmembrane transport
F	0140359	molecular_function	ABC-type transporter activity
G	0005524	molecular_function	ATP binding
G	0016020	cellular_component	membrane
G	0016887	molecular_function	ATP hydrolysis activity
G	0055085	biological_process	transmembrane transport
G	0140359	molecular_function	ABC-type transporter activity
H	0005524	molecular_function	ATP binding
H	0016020	cellular_component	membrane
H	0016887	molecular_function	ATP hydrolysis activity
H	0055085	biological_process	transmembrane transport
H	0140359	molecular_function	ABC-type transporter activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue ADP A 1001

Chain	Residue
A	TYR481
A	THR515
A	MG1002
B	THR611
A	YCM483
A	VAL489
A	SER509
A	GLY510
A	GLY511
A	GLY512
A	LYS513
A	THR514

site_id	AC2
Number of Residues	2
Details	binding site for residue MG A 1002

Chain	Residue
A	THR514
A	ADP1001

site_id	AC3
Number of Residues	6
Details	binding site for residue Y01 A 1003

Chain	Residue
A	PRO303
A	SER382
A	ASN383
A	GLN422
A	MET425
A	LEU428

site_id	AC4
Number of Residues	12
Details	binding site for residue ADP B 1001

Chain	Residue
A	THR611
B	TYR481
B	YCM483
B	VAL489
B	SER509
B	GLY510
B	GLY511
B	GLY512
B	LYS513
B	THR514
B	THR515
B	MG1002

site_id	AC5
Number of Residues	2
Details	binding site for residue MG B 1002

Chain	Residue
B	THR514
B	ADP1001

site_id	AC6
Number of Residues	8
Details	binding site for residue Y01 B 1003

Chain	Residue
B	TRP134
B	PRO303
B	SER382
B	ASN383
B	GLN422
B	MET425
B	LEU428
B	VAL435

site_id	AC7
Number of Residues	12
Details	binding site for residue ADP C 1001

Chain	Residue
C	TYR481
C	YCM483
C	PHE487
C	SER509
C	GLY510
C	GLY511
C	GLY512
C	LYS513
C	THR514
C	THR515
C	MG1002
D	THR611

site_id	AC8
Number of Residues	3
Details	binding site for residue MG C 1002

Chain	Residue
C	THR514
C	ASP636
C	ADP1001

site_id	AC9
Number of Residues	12
Details	binding site for residue ADP D 1001

Chain	Residue
C	THR611
D	TYR481
D	YCM483
D	VAL489
D	SER509
D	GLY510
D	GLY511
D	GLY512
D	LYS513
D	THR514
D	THR515
D	MG1002

site_id	AD1
Number of Residues	3
Details	binding site for residue MG D 1002

Chain	Residue
D	THR514
D	ASP636
D	ADP1001

site_id	AD2
Number of Residues	4
Details	binding site for residue Y01 D 1003

Chain	Residue
D	PRO303
D	SER382
D	MET425
D	LEU428

site_id	AD3
Number of Residues	10
Details	binding site for residue ADP E 1001

Chain	Residue
E	TYR481
E	YCM483
E	SER509
E	GLY510
E	GLY511
E	GLY512
E	LYS513
E	THR514
E	THR515
E	MG1002

site_id	AD4
Number of Residues	3
Details	binding site for residue MG E 1002

Chain	Residue
E	THR514
E	ASP636
E	ADP1001

site_id	AD5
Number of Residues	7
Details	binding site for residue Y01 E 1003

Chain	Residue
E	PRO303
E	SER382
E	ASN383
E	GLN422
E	MET425
E	LEU428
E	VAL435

site_id	AD6
Number of Residues	12
Details	binding site for residue ADP F 1001

Chain	Residue
F	VAL489
F	SER509
F	GLY510
F	GLY511
F	GLY512
F	LYS513
F	THR514
F	THR515
F	MG1002
E	THR611
F	TYR481
F	YCM483

site_id	AD7
Number of Residues	2
Details	binding site for residue MG F 1002

Chain	Residue
F	THR514
F	ADP1001

site_id	AD8
Number of Residues	8
Details	binding site for residue Y01 F 1003

Chain	Residue
F	TRP134
F	PRO303
F	SER382
F	ASN383
F	GLN422
F	MET425
F	LEU428
F	VAL435

site_id	AD9
Number of Residues	11
Details	binding site for residue ADP G 1001

Chain	Residue
G	TYR481
G	YCM483
G	VAL489
G	SER509
G	GLY510
G	GLY511
G	GLY512
G	LYS513
G	THR514
G	THR515
G	MG1002

site_id	AE1
Number of Residues	3
Details	binding site for residue MG G 1002

Chain	Residue
G	THR514
G	ASP636
G	ADP1001

site_id	AE2
Number of Residues	2
Details	binding site for residue Y01 G 1003

Chain	Residue
G	MET425
G	LEU428

site_id	AE3
Number of Residues	10
Details	binding site for residue ADP H 1001

Chain	Residue
G	THR611
H	TYR481
H	SER509
H	GLY510
H	GLY511
H	GLY512
H	LYS513
H	THR514
H	THR515
H	MG1002

site_id	AE4
Number of Residues	3
Details	binding site for residue MG H 1002

Chain	Residue
H	THR514
H	ASP636
H	ADP1001

site_id	AE5
Number of Residues	5
Details	binding site for residue Y01 H 1003

Chain	Residue
H	PRO303
H	SER382
H	ASN383
H	MET425
H	LEU428

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
F	LEU612-LEU626
E	LEU612-LEU626
H	LEU612-LEU626
A	LEU612-LEU626
B	LEU612-LEU626

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	460
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2017","submissionDatabase":"PDB data bank","title":"The crystal structure of human ABCB8 in an outward-facing state.","authors":["Faust B.","Pike A.C.W.","Shintre C.A.","Quiqley A.M.","Chu A.","Barr A.","Shrestha L.","Mukhopadhyay S.","Borkowska O.","Chalk R.","Burgess-Brown N.A.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Carpenter E.P."]}},{"source":"PDB","id":"5OCH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	312
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"31435016","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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