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6NC9

Lipid II flippase MurJ, outward-facing conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0015648molecular_functionlipid-linked peptidoglycan transporter activity
A0015836biological_processlipid-linked peptidoglycan transport
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue 1PE A 501
ChainResidue
ATYR285
AASN288
AASP289
ALYS292
AASP416
AOLB506

site_idAC2
Number of Residues9
Detailsbinding site for residue OLB A 502
ChainResidue
ALEU126
APRO130
AILE178
AOLC511
AHOH606
AHOH716
ATYR36
AGLU37
ALYS123

site_idAC3
Number of Residues8
Detailsbinding site for residue OLB A 503
ChainResidue
AILE306
APHE307
ASER309
ATHR310
APRO311
ASER331
AOLC515
AHOH605

site_idAC4
Number of Residues8
Detailsbinding site for residue OLB A 504
ChainResidue
ALYS419
APHE461
ATYR462
AARG463
AASP464
ALEU465
AHOH604
AHOH751

site_idAC5
Number of Residues7
Detailsbinding site for residue OLB A 505
ChainResidue
AALA93
AILE208
APHE211
APRO212
APHE241
AILE379
AOLC512

site_idAC6
Number of Residues8
Detailsbinding site for residue OLB A 506
ChainResidue
ALEU4
AASP289
ATHR293
APHE296
ATYR462
ALEU465
A1PE501
AOLC510

site_idAC7
Number of Residues5
Detailsbinding site for residue OLB A 507
ChainResidue
ATHR164
AGLY168
ATYR175
ASER179
AOLC511

site_idAC8
Number of Residues7
Detailsbinding site for residue OLB A 508
ChainResidue
AILE43
AALA44
AMET46
APHE47
APRO48
AILE106
AILE132

site_idAC9
Number of Residues6
Detailsbinding site for residue NA A 509
ChainResidue
AASP235
AASN374
AASP378
AVAL390
AALA393
ATHR394

site_idAD1
Number of Residues5
Detailsbinding site for residue OLC A 510
ChainResidue
ASER2
APHE5
ALEU465
APHE469
AOLB506

site_idAD2
Number of Residues4
Detailsbinding site for residue OLC A 511
ChainResidue
AILE178
ATYR385
AOLB502
AOLB507

site_idAD3
Number of Residues4
Detailsbinding site for residue OLC A 512
ChainResidue
AILE379
AILE380
ALEU383
AOLB505

site_idAD4
Number of Residues5
Detailsbinding site for residue OLC A 513
ChainResidue
ATRP153
ATHR157
AILE160
ASER194
AHOH693

site_idAD5
Number of Residues1
Detailsbinding site for residue OLC A 515
ChainResidue
AOLB503

site_idAD6
Number of Residues3
Detailsbinding site for residue OLC A 516
ChainResidue
AMET46
APHE50
APHE109

site_idAD7
Number of Residues7
Detailsbinding site for residue OLC A 517
ChainResidue
AASN85
ASER88
ALEU89
ALEU92
APHE206
ATHR207
AILE208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues87
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28024149
ChainResidueDetails
AMET1-SER2
AGLU57-LYS78
ALEU145-LYS150
ALYS197-HIS213
AVAL272-LEU287
ATYR354-THR362
ASER408-ASP416
ATYR462-LYS475

site_idSWS_FT_FI2
Number of Residues285
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:28024149
ChainResidueDetails
AILE3-PHE23
AILE333-SER353
APRO363-LEU383
APRO387-PHE407
APHE417-THR437
APHE441-PHE461
ATYR36-GLY56
APHE79-TYR99
ALEU124-ILE144
APHE151-LEU171
AGLY176-ILE196
APHE214-VAL238
ALEU250-VAL271
AASN288-LEU308

site_idSWS_FT_FI3
Number of Residues74
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:28024149
ChainResidueDetails
AARG24-SER35
APHE100-LYS123
ASER172-TYR175
AVAL239-TYR249
ASER309-LYS332
ALYS384-GLY386
AASP438-GLU440

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PDB entries from 2024-07-24

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