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7CH6

Cryo-EM structure of E.coli MlaFEB with AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005548molecular_functionphospholipid transporter activity
A0005886cellular_componentplasma membrane
A0015914biological_processphospholipid transport
A0016020cellular_componentmembrane
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0120010biological_processintermembrane phospholipid transfer
A0120014molecular_functionphospholipid transfer activity
A1990531cellular_componentphospholipid-translocating ATPase complex
B0005515molecular_functionprotein binding
B0005548molecular_functionphospholipid transporter activity
B0005886cellular_componentplasma membrane
B0015914biological_processphospholipid transport
B0016020cellular_componentmembrane
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0120010biological_processintermembrane phospholipid transfer
B0120014molecular_functionphospholipid transfer activity
B1990531cellular_componentphospholipid-translocating ATPase complex
C0000166molecular_functionnucleotide binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006869biological_processlipid transport
C0015914biological_processphospholipid transport
C0016020cellular_componentmembrane
C0016887molecular_functionATP hydrolysis activity
C0120010biological_processintermembrane phospholipid transfer
C0120014molecular_functionphospholipid transfer activity
C1990531cellular_componentphospholipid-translocating ATPase complex
D0000166molecular_functionnucleotide binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005886cellular_componentplasma membrane
D0006869biological_processlipid transport
D0015914biological_processphospholipid transport
D0016020cellular_componentmembrane
D0016887molecular_functionATP hydrolysis activity
D0120010biological_processintermembrane phospholipid transfer
D0120014molecular_functionphospholipid transfer activity
D1990531cellular_componentphospholipid-translocating ATPase complex
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006974biological_processDNA damage response
E0015914biological_processphospholipid transport
E0016020cellular_componentmembrane
E0046677biological_processresponse to antibiotic
E0120010biological_processintermembrane phospholipid transfer
E0120014molecular_functionphospholipid transfer activity
E1990531cellular_componentphospholipid-translocating ATPase complex
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006974biological_processDNA damage response
F0015914biological_processphospholipid transport
F0016020cellular_componentmembrane
F0046677biological_processresponse to antibiotic
F0120010biological_processintermembrane phospholipid transfer
F0120014molecular_functionphospholipid transfer activity
F1990531cellular_componentphospholipid-translocating ATPase complex
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue ANP C 301
ChainResidue
CARG18
CGLU170
CARG21
CILE23
CGLY44
CILE45
CGLY46
CLYS47
CTHR48
CGLN92

site_idAC2
Number of Residues10
Detailsbinding site for residue ANP D 301
ChainResidue
DARG18
DARG21
DILE23
DGLY44
DILE45
DGLY46
DLYS47
DTHR48
DGLN92
DGLU170

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGMARRAALARAI
ChainResidueDetails
CLEU145-ILE159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues200
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues90
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues110
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues472
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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