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9NXC

Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.

Functional Information from GO Data
ChainGOidnamespacecontents
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0015423molecular_functionABC-type maltose transporter activity
C0043190cellular_componentATP-binding cassette (ABC) transporter complex
C0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
C0140359molecular_functionABC-type transporter activity
C1904981biological_processmaltose transmembrane transport
C1990060cellular_componentmaltose transport complex
D0000166molecular_functionnucleotide binding
D0005524molecular_functionATP binding
D0005886cellular_componentplasma membrane
D0015423molecular_functionABC-type maltose transporter activity
D0043190cellular_componentATP-binding cassette (ABC) transporter complex
D0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
D0140359molecular_functionABC-type transporter activity
D1904981biological_processmaltose transmembrane transport
D1990060cellular_componentmaltose transport complex
H0005886cellular_componentplasma membrane
H0015423molecular_functionABC-type maltose transporter activity
H0042956biological_processmaltodextrin transmembrane transport
H1904981biological_processmaltose transmembrane transport
H1990060cellular_componentmaltose transport complex
I0005886cellular_componentplasma membrane
I0015423molecular_functionABC-type maltose transporter activity
I0015768biological_processmaltose transport
I0042956biological_processmaltodextrin transmembrane transport
I1904981biological_processmaltose transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRVAIGRTL
ChainResidueDetails
CLEU134-LEU148
DLEU134-LEU148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues261
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues163
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues420
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues460
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"HAMAP-Rule","id":"MF_01709","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01709","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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