Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4DBL

Crystal structure of E159Q mutant of BtuCDF

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0015420	molecular_function	ABC-type vitamin B12 transporter activity
A	0015889	biological_process	cobalamin transport
A	0016020	cellular_component	membrane
A	0022857	molecular_function	transmembrane transporter activity
A	0035461	biological_process	vitamin transmembrane transport
A	0042802	molecular_function	identical protein binding
A	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
A	0055085	biological_process	transmembrane transport
A	0090482	molecular_function	vitamin transmembrane transporter activity
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
B	0015420	molecular_function	ABC-type vitamin B12 transporter activity
B	0015889	biological_process	cobalamin transport
B	0016020	cellular_component	membrane
B	0022857	molecular_function	transmembrane transporter activity
B	0035461	biological_process	vitamin transmembrane transport
B	0042802	molecular_function	identical protein binding
B	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
B	0055085	biological_process	transmembrane transport
B	0090482	molecular_function	vitamin transmembrane transporter activity
C	0000166	molecular_function	nucleotide binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005886	cellular_component	plasma membrane
C	0015420	molecular_function	ABC-type vitamin B12 transporter activity
C	0015889	biological_process	cobalamin transport
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0019898	cellular_component	extrinsic component of membrane
C	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
C	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
C	0055085	biological_process	transmembrane transport
D	0000166	molecular_function	nucleotide binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005886	cellular_component	plasma membrane
D	0015420	molecular_function	ABC-type vitamin B12 transporter activity
D	0015889	biological_process	cobalamin transport
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0019898	cellular_component	extrinsic component of membrane
D	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
D	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
D	0055085	biological_process	transmembrane transport
E	0015889	biological_process	cobalamin transport
E	0031419	molecular_function	cobalamin binding
E	0042597	cellular_component	periplasmic space
F	0005515	molecular_function	protein binding
F	0005886	cellular_component	plasma membrane
F	0015420	molecular_function	ABC-type vitamin B12 transporter activity
F	0015889	biological_process	cobalamin transport
F	0016020	cellular_component	membrane
F	0022857	molecular_function	transmembrane transporter activity
F	0035461	biological_process	vitamin transmembrane transport
F	0042802	molecular_function	identical protein binding
F	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
F	0055085	biological_process	transmembrane transport
F	0090482	molecular_function	vitamin transmembrane transporter activity
G	0005515	molecular_function	protein binding
G	0005886	cellular_component	plasma membrane
G	0015420	molecular_function	ABC-type vitamin B12 transporter activity
G	0015889	biological_process	cobalamin transport
G	0016020	cellular_component	membrane
G	0022857	molecular_function	transmembrane transporter activity
G	0035461	biological_process	vitamin transmembrane transport
G	0042802	molecular_function	identical protein binding
G	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
G	0055085	biological_process	transmembrane transport
G	0090482	molecular_function	vitamin transmembrane transporter activity
H	0000166	molecular_function	nucleotide binding
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005886	cellular_component	plasma membrane
H	0015420	molecular_function	ABC-type vitamin B12 transporter activity
H	0015889	biological_process	cobalamin transport
H	0016020	cellular_component	membrane
H	0016887	molecular_function	ATP hydrolysis activity
H	0019898	cellular_component	extrinsic component of membrane
H	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
H	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
H	0055085	biological_process	transmembrane transport
I	0000166	molecular_function	nucleotide binding
I	0005515	molecular_function	protein binding
I	0005524	molecular_function	ATP binding
I	0005886	cellular_component	plasma membrane
I	0015420	molecular_function	ABC-type vitamin B12 transporter activity
I	0015889	biological_process	cobalamin transport
I	0016020	cellular_component	membrane
I	0016887	molecular_function	ATP hydrolysis activity
I	0019898	cellular_component	extrinsic component of membrane
I	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
I	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
I	0055085	biological_process	transmembrane transport
J	0015889	biological_process	cobalamin transport
J	0031419	molecular_function	cobalamin binding
J	0042597	cellular_component	periplasmic space

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 C 301

Chain	Residue
C	PRO34
C	ASN35
C	GLY36
C	ALA37
C	GLY38
C	LYS39
C	SER40

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 302

Chain	Residue
C	ARG217
C	ARG243

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 303

Chain	Residue
C	ARG198
C	HIS199
C	ALA200
C	HIS201
C	ARG217

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 304

Chain	Residue
C	ARG202
C	ARG216

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 301

Chain	Residue
D	PRO34
D	ASN35
D	GLY36
D	ALA37
D	GLY38
D	LYS39
D	SER40

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 302

Chain	Residue
D	ARG202
D	ARG216

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 303

Chain	Residue
D	ARG217
D	ARG243
D	SO4304

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 304

Chain	Residue
D	ARG198
D	HIS199
D	HIS201
D	ARG217
D	SO4303

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 H 301

Chain	Residue
H	GLY36
H	ALA37
H	GLY38
H	LYS39
H	SER40

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 H 302

Chain	Residue
H	ARG217
H	ARG243

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 H 303

Chain	Residue
H	ARG198
H	HIS201
H	ARG217

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 H 304

Chain	Residue
H	ARG202
H	ARG216

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 I 301

Chain	Residue
I	GLY36
I	ALA37
I	GLY38
I	LYS39
I	SER40

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 I 302

Chain	Residue
I	ARG202
I	ARG216

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 I 303

Chain	Residue
I	ARG217
I	ARG243

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 I 304

Chain	Residue
I	ARG198
I	HIS201
I	ARG217

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	LEU127-VAL141

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	192
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	96
Details	Transmembrane: {"description":"Helical; Name=1"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	248
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	96
Details	Transmembrane: {"description":"Helical; Name=2"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	56
Details	Transmembrane: {"description":"Helical; Name=3"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	96
Details	Transmembrane: {"description":"Helical; Name=4"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	96
Details	Transmembrane: {"description":"Helical; Name=5"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=6"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	80
Details	Transmembrane: {"description":"Helical; Name=7"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	36
Details	Transmembrane: {"description":"Helical; Name=8"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=9"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	76
Details	Transmembrane: {"description":"Helical; Name=10"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01005","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	482
Details	Domain: {"description":"Fe/B12 periplasmic-binding","evidences":[{"source":"HAMAP-Rule","id":"MF_01000","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01000","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12468528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N4A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01000","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12468528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12475936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1N4A","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Site: {"description":"Important for BtuC binding","evidences":[{"source":"HAMAP-Rule","id":"MF_01000","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12475936","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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