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6NC6

Lipid II flippase MurJ, inward closed 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
A0016020cellular_componentmembrane
A0034204biological_processlipid translocation
A0071555biological_processcell wall organization
B0005886cellular_componentplasma membrane
B0008360biological_processregulation of cell shape
B0009252biological_processpeptidoglycan biosynthetic process
B0015648molecular_functionlipid-linked peptidoglycan transporter activity
B0015836biological_processlipid-linked peptidoglycan transport
B0016020cellular_componentmembrane
B0034204biological_processlipid translocation
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 501
ChainResidue
AASP235
AASN374
AASP378
AVAL390
AALA393
ATHR394

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 502
ChainResidue
ATYR41
AILE45
AARG255

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 503
ChainResidue
ALYS71
AHIS210
AHIS213
ACL504
AZN505

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 504
ChainResidue
AHIS210
AHIS213
ACL503
AZN505

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 505
ChainResidue
AHIS210
AHIS213
ACL503
ACL504

site_idAC6
Number of Residues6
Detailsbinding site for residue OLB A 506
ChainResidue
ATYR175
AILE178
ASER179
AILE182
AGLY183
BGLU70

site_idAC7
Number of Residues2
Detailsbinding site for residue CL B 501
ChainResidue
BTYR41
BARG255

site_idAC8
Number of Residues5
Detailsbinding site for residue CL B 502
ChainResidue
BLYS71
BHIS210
BHIS213
BCL503
BZN504

site_idAC9
Number of Residues4
Detailsbinding site for residue CL B 503
ChainResidue
BLYS71
BHIS210
BCL502
BZN504

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 504
ChainResidue
BHIS210
BHIS213
BCL502
BCL503

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues174
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28024149
ChainResidueDetails
AMET1-SER2
AGLU57-LYS78
ALEU145-LYS150
ALYS197-HIS213
AVAL272-LEU287
ATYR354-THR362
ASER408-ASP416
ATYR462-LYS475
BMET1-SER2
BGLU57-LYS78
BLEU145-LYS150
BLYS197-HIS213
BVAL272-LEU287
BTYR354-THR362
BSER408-ASP416
BTYR462-LYS475

site_idSWS_FT_FI2
Number of Residues570
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:28024149
ChainResidueDetails
AILE3-PHE23
ATYR36-GLY56
APHE79-TYR99
ALEU124-ILE144
APHE151-LEU171
AGLY176-ILE196
APHE214-VAL238
ALEU250-VAL271
AASN288-LEU308
AILE333-SER353
APRO363-LEU383
APRO387-PHE407
APHE417-THR437
APHE441-PHE461
BILE3-PHE23
BTYR36-GLY56
BPHE79-TYR99
BLEU124-ILE144
BPHE151-LEU171
BGLY176-ILE196
BPHE214-VAL238
BLEU250-VAL271
BASN288-LEU308
BILE333-SER353
BPRO363-LEU383
BPRO387-PHE407
BPHE417-THR437
BPHE441-PHE461

site_idSWS_FT_FI3
Number of Residues148
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:28024149
ChainResidueDetails
AARG24-SER35
APHE100-LYS123
ASER172-TYR175
AVAL239-TYR249
ASER309-LYS332
ALYS384-GLY386
AASP438-GLU440
BARG24-SER35
BPHE100-LYS123
BSER172-TYR175
BVAL239-TYR249
BSER309-LYS332
BLYS384-GLY386
BASP438-GLU440

218500

PDB entries from 2024-04-17

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