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4R9U

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0015420molecular_functionABC-type vitamin B12 transporter activity
A0015889biological_processcobalamin transport
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0035461biological_processvitamin transmembrane transport
A0042802molecular_functionidentical protein binding
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055085biological_processtransmembrane transport
A0090482molecular_functionvitamin transmembrane transporter activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0015420molecular_functionABC-type vitamin B12 transporter activity
B0015889biological_processcobalamin transport
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0035461biological_processvitamin transmembrane transport
B0042802molecular_functionidentical protein binding
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0055085biological_processtransmembrane transport
B0090482molecular_functionvitamin transmembrane transporter activity
C0000166molecular_functionnucleotide binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0015420molecular_functionABC-type vitamin B12 transporter activity
C0015889biological_processcobalamin transport
C0016020cellular_componentmembrane
C0016887molecular_functionATP hydrolysis activity
C0019898cellular_componentextrinsic component of membrane
C0042626molecular_functionATPase-coupled transmembrane transporter activity
C0043190cellular_componentATP-binding cassette (ABC) transporter complex
C0055085biological_processtransmembrane transport
D0000166molecular_functionnucleotide binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005886cellular_componentplasma membrane
D0015420molecular_functionABC-type vitamin B12 transporter activity
D0015889biological_processcobalamin transport
D0016020cellular_componentmembrane
D0016887molecular_functionATP hydrolysis activity
D0019898cellular_componentextrinsic component of membrane
D0042626molecular_functionATPase-coupled transmembrane transporter activity
D0043190cellular_componentATP-binding cassette (ABC) transporter complex
D0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LDA A 501
ChainResidue
ATRP115
AARG189
ATRP192

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LDA A 502
ChainResidue
ATRP188

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LDA B 501
ChainResidue
BTRP192

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LDA B 502
ChainResidue
BTRP188

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ANP C 301
ChainResidue
CGLY38
CLYS39
CSER40
CTHR41
CGLN80
CGLN159
CHIS191
CMG302
DARG122
DGLN126
DSER128
DGLY129
DGLY130
DGLU131
DSER163
CARG15
CASN35
CGLY36

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 302
ChainResidue
CSER40
CGLN80
CANP301

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ANP D 301
ChainResidue
CARG122
CSER128
CGLY129
CGLY130
CGLU131
CSER163
DARG15
DASN35
DGLY36
DGLY38
DLYS39
DSER40
DTHR41
DGLN80
DHIS191
DMG302

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG D 302
ChainResidue
DSER40
DGLN80
DANP301

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGEWQRVRLAAVV
ChainResidueDetails
CLEU127-VAL141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues96
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues124
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues30
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=8"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=9"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=10"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01005","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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