Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4FI3

Structure of vitamin B12 transporter BtuCD-F in a nucleotide-bound state

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
F	0015889	biological_process	cobalamin transport
F	0031419	molecular_function	cobalamin binding
F	0042597	cellular_component	periplasmic space

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ANP C 301

Chain	Residue
C	ARG15
C	GLN159
C	HIS191
C	MG302
D	ARG122
D	GLN126
D	LEU127
D	SER128
D	GLY129
D	GLY130
D	GLU131
C	PRO34
C	ASN35
C	GLY36
C	ALA37
C	GLY38
C	LYS39
C	SER40
C	THR41

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 302

Chain	Residue
C	SER40
C	GLN80
C	GLN159
C	ANP301

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ANP D 301

Chain	Residue
C	ARG122
C	GLN126
C	SER128
C	GLY129
C	GLY130
C	GLU131
D	ARG15
D	PRO34
D	ASN35
D	GLY36
D	ALA37
D	GLY38
D	LYS39
D	SER40
D	THR41
D	GLN159
D	HIS191
D	MG302

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 302

Chain	Residue
D	SER40
D	GLN80
D	GLN159
D	ANP301

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	96
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	48
Details	Transmembrane: {"description":"Helical; Name=1"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	124
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	48
Details	Transmembrane: {"description":"Helical; Name=2"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	28
Details	Transmembrane: {"description":"Helical; Name=3"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	48
Details	Transmembrane: {"description":"Helical; Name=4"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	48
Details	Transmembrane: {"description":"Helical; Name=5"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	30
Details	Transmembrane: {"description":"Helical; Name=6"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=7"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	18
Details	Transmembrane: {"description":"Helical; Name=8"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	42
Details	Transmembrane: {"description":"Helical; Name=9"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	38
Details	Transmembrane: {"description":"Helical; Name=10"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01005","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	241
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	1
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	4
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	2
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)