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6S8N

Cryo-EM structure of LptB2FGC in complex with lipopolysaccharide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0016887molecular_functionATP hydrolysis activity
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055085biological_processtransmembrane transport
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0016887molecular_functionATP hydrolysis activity
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0055085biological_processtransmembrane transport
C0005886cellular_componentplasma membrane
C0015221molecular_functionlipopolysaccharide transmembrane transporter activity
C0015920biological_processlipopolysaccharide transport
C0017089molecular_functionglycolipid transfer activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
C0046836biological_processglycolipid 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 Residues7
Detailsbinding site for residue DCQ B 301
ChainResidue
BARG91
BMET134
BGLY135
BGLN136
FLYS78
FTHR81
FGLU82

site_idAC2
Number of Residues8
Detailsbinding site for residue LMN F 401
ChainResidue
CILE10
CSER13
FLEU297
GILE32
GL0W401
GLMN402
CMET1
CARG6

site_idAC3
Number of Residues4
Detailsbinding site for residue LMT F 402
ChainResidue
FARG295
FMET299
GLMT403
GDCQ404

site_idAC4
Number of Residues10
Detailsbinding site for residue L0W G 401
ChainResidue
FILE25
FARG33
FLMN401
GILE66
GPHE67
GPRO69
GSER314
GPHE317
GPHE319
GTYR320

site_idAC5
Number of Residues7
Detailsbinding site for residue LMN G 402
ChainResidue
FGLN293
FGLY294
FLMN401
GMET25
GPRO304
GMET305
GGLY306

site_idAC6
Number of Residues4
Detailsbinding site for residue LMT G 403
ChainResidue
FLMT402
GPRO299
GLEU300
GVAL307

site_idAC7
Number of Residues2
Detailsbinding site for residue DCQ G 404
ChainResidue
FLMT402
GSER314

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 Residues18
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_01915
ChainResidueDetails
CTRP7-ALA25
BGLY36
FPRO291-ARG295
FASP349-VAL366

site_idSWS_FT_FI2
Number of Residues120
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
FLEU16-GLY36
FLEU54-MET74
FALA101-GLY121
FILE270-ASN290
FVAL296-LEU316
FTHR328-TRP348

site_idSWS_FT_FI3
Number of Residues173
DetailsTOPO_DOM: Periplasmic => ECO:0000255
ChainResidueDetails
FALA37-GLY53
FPRO122-ARG269
FLYS317-PRO327

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PDB entries from 2024-10-30

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