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6S8G

Cryo-EM structure of LptB2FGC in complex with AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0016887molecular_functionATP hydrolysis activity
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055085biological_processtransmembrane transport
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0016887molecular_functionATP hydrolysis activity
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0055085biological_processtransmembrane transport
F0005886cellular_componentplasma membrane
F0015920biological_processlipopolysaccharide transport
F0016020cellular_componentmembrane
F0043190cellular_componentATP-binding cassette (ABC) transporter complex
F0055085biological_processtransmembrane transport
G0005886cellular_componentplasma membrane
G0015920biological_processlipopolysaccharide transport
G0016020cellular_componentmembrane
G0043190cellular_componentATP-binding cassette (ABC) transporter complex
G0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ANP A 401
ChainResidue
ATYR13
AGLN85
BSER137
BSER139
BGLY141
BGLU142
GARG301
AARG16
AVAL18
AASN38
AGLY39
AGLY41
ALYS42
ATHR43
ATHR44

site_idAC2
Number of Residues15
Detailsbinding site for residue ANP B 401
ChainResidue
ASER137
ASER139
AGLY141
AGLU142
BTYR13
BARG16
BVAL18
BASN38
BGLY39
BGLY41
BLYS42
BTHR43
BTHR44
BGLN85
FARG292

site_idAC3
Number of Residues1
Detailsbinding site for residue LMD F 501
ChainResidue
FLYS13

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGERRRVEIARAL
ChainResidueDetails
ALEU138-LEU152

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues466
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues120
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues26
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues29
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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