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6SN3

BamABCDE in MSP1D1 nanodisc ensemble 0-3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0007155biological_processcell adhesion
A0009279cellular_componentcell outer membrane
A0016020cellular_componentmembrane
A0019867cellular_componentouter membrane
A0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
A0051205biological_processprotein insertion into membrane
A0071709biological_processmembrane assembly
A1990063cellular_componentBam protein complex
B0005515molecular_functionprotein binding
B0009279cellular_componentcell outer membrane
B0016020cellular_componentmembrane
B0042802molecular_functionidentical protein binding
B0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
B0051205biological_processprotein insertion into membrane
B1990063cellular_componentBam protein complex
D0005515molecular_functionprotein binding
D0009279cellular_componentcell outer membrane
D0016020cellular_componentmembrane
D0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
D0051205biological_processprotein insertion into membrane
D1990063cellular_componentBam protein complex
E0005515molecular_functionprotein binding
E0009279cellular_componentcell outer membrane
E0016020cellular_componentmembrane
E0019867cellular_componentouter membrane
E0030674molecular_functionprotein-macromolecule adaptor activity
E0042802molecular_functionidentical protein binding
E0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
E0046677biological_processresponse to antibiotic
E0051205biological_processprotein insertion into membrane
E1901612molecular_functioncardiolipin binding
E1990063cellular_componentBam protein complex
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DINQGNYLTanDV
ChainResidueDetails
EASP31-VAL43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsLIPID: S-diacylglycerol cysteine => ECO:0000255|HAMAP-Rule:MF_00924, ECO:0000269|PubMed:1885529, ECO:0000305|PubMed:27686148
ChainResidueDetails
CCYS25

site_idSWS_FT_FI2
Number of Residues1
DetailsTOPO_DOM: Extracellular; loop 1 => ECO:0000305
ChainResidueDetails
ATHR434-GLU435

site_idSWS_FT_FI3
Number of Residues10
DetailsTRANSMEM: Beta stranded; Name=Strand 2 => ECO:0000269|PubMed:24914988
ChainResidueDetails
ASER436-GLN446

site_idSWS_FT_FI4
Number of Residues63
DetailsTOPO_DOM: Periplasmic => ECO:0000305
ChainResidueDetails
AASP447-TYR454
APRO476-VAL483
ALYS507-TYR522
ATYR578-GLY590
APRO620-VAL628
AILE719-SER732
ASER778

site_idSWS_FT_FI5
Number of Residues7
DetailsTRANSMEM: Beta stranded; Name=Strand 3 => ECO:0000269|PubMed:24914988
ChainResidueDetails
AALA455-LYS462

site_idSWS_FT_FI6
Number of Residues2
DetailsTOPO_DOM: Extracellular; loop 2 => ECO:0000305
ChainResidueDetails
AASN463-TYR465

site_idSWS_FT_FI7
Number of Residues9
DetailsTRANSMEM: Beta stranded; Name=Strand 4 => ECO:0000269|PubMed:24914988
ChainResidueDetails
AGLN466-ASN475

site_idSWS_FT_FI8
Number of Residues11
DetailsTRANSMEM: Beta stranded; Name=Strand 5 => ECO:0000269|PubMed:24914988
ChainResidueDetails
ASER484-GLN495

site_idSWS_FT_FI9
Number of Residues8
DetailsTOPO_DOM: Extracellular; loop 3 => ECO:0000305
ChainResidueDetails
AALA496-TYR504

site_idSWS_FT_FI10
Number of Residues1
DetailsTRANSMEM: Beta stranded; Name=Strand 6 => ECO:0000269|PubMed:24914988
ChainResidueDetails
ATHR505-ASN506

site_idSWS_FT_FI11
Number of Residues12
DetailsTRANSMEM: Beta stranded; Name=Strand 7 => ECO:0000269|PubMed:24914988
ChainResidueDetails
AASN523-SER535

site_idSWS_FT_FI12
Number of Residues27
DetailsTOPO_DOM: Extracellular; loop 4 => ECO:0000269|PubMed:23882017, ECO:0000269|PubMed:24914988
ChainResidueDetails
ALEU536-ASN563

site_idSWS_FT_FI13
Number of Residues13
DetailsTRANSMEM: Beta stranded; Name=Strand 8 => ECO:0000269|PubMed:24914988
ChainResidueDetails
ASER564-THR577

site_idSWS_FT_FI14
Number of Residues9
DetailsTRANSMEM: Beta stranded; Name=Strand 9 => ECO:0000269|PubMed:24914988
ChainResidueDetails
ASER591-THR600

site_idSWS_FT_FI15
Number of Residues7
DetailsTOPO_DOM: Extracellular; loop 5 => ECO:0000305
ChainResidueDetails
AILE601-TYR608

site_idSWS_FT_FI16
Number of Residues10
DetailsTRANSMEM: Beta stranded; Name=Strand 10 => ECO:0000269|PubMed:24914988
ChainResidueDetails
ATYR609-VAL619

site_idSWS_FT_FI17
Number of Residues10
DetailsTRANSMEM: Beta stranded; Name=Strand 11 => ECO:0000269|PubMed:24914988
ChainResidueDetails
AVAL629-ASP639

site_idSWS_FT_FI18
Number of Residues68
DetailsTOPO_DOM: Extracellular; loop 6 => ECO:0000269|PubMed:23882017, ECO:0000269|PubMed:24914988
ChainResidueDetails
AGLY640-GLY708

site_idSWS_FT_FI19
Number of Residues9
DetailsTRANSMEM: Beta stranded; Name=Strand 12 => ECO:0000269|PubMed:24914988
ChainResidueDetails
AASN709-PHE718

site_idSWS_FT_FI20
Number of Residues12
DetailsTRANSMEM: Beta stranded; Name=Strand 13 => ECO:0000269|PubMed:24914988
ChainResidueDetails
AVAL733-TRP745

site_idSWS_FT_FI21
Number of Residues21
DetailsTOPO_DOM: Extracellular; loop 7 => ECO:0000305
ChainResidueDetails
AASP746-ARG767

site_idSWS_FT_FI22
Number of Residues9
DetailsTRANSMEM: Beta stranded; Name=Strand 14 => ECO:0000269|PubMed:24914988
ChainResidueDetails
AMET768-MET777

site_idSWS_FT_FI23
Number of Residues10
DetailsTRANSMEM: Beta stranded; Name=Strand 15 => ECO:0000269|PubMed:24914988
ChainResidueDetails
APRO779-GLN789

site_idSWS_FT_FI24
Number of Residues13
DetailsTOPO_DOM: Extracellular; loop 8 => ECO:0000305
ChainResidueDetails
APRO790-GLN803

227344

PDB entries from 2024-11-13

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