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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8CXR

Crystal structure of MraY bound to a sphaerimicin analogue

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008360biological_processregulation of cell shape
A0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
A0042802molecular_functionidentical protein binding
A0044038biological_processcell wall macromolecule biosynthetic process
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0051992molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
A0071555biological_processcell wall organization
B0005886cellular_componentplasma membrane
B0008360biological_processregulation of cell shape
B0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
B0042802molecular_functionidentical protein binding
B0044038biological_processcell wall macromolecule biosynthetic process
B0046872molecular_functionmetal ion binding
B0051301biological_processcell division
B0051992molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
B0071555biological_processcell wall organization
C0005886cellular_componentplasma membrane
C0008360biological_processregulation of cell shape
C0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016020cellular_componentmembrane
C0016740molecular_functiontransferase activity
C0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
C0042802molecular_functionidentical protein binding
C0044038biological_processcell wall macromolecule biosynthetic process
C0046872molecular_functionmetal ion binding
C0051301biological_processcell division
C0051992molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
C0071555biological_processcell wall organization
D0005886cellular_componentplasma membrane
D0008360biological_processregulation of cell shape
D0008963molecular_functionphospho-N-acetylmuramoyl-pentapeptide-transferase activity
D0009252biological_processpeptidoglycan biosynthetic process
D0016020cellular_componentmembrane
D0016740molecular_functiontransferase activity
D0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
D0042802molecular_functionidentical protein binding
D0044038biological_processcell wall macromolecule biosynthetic process
D0046872molecular_functionmetal ion binding
D0051301biological_processcell division
D0051992molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
D0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS01347
Number of Residues13
DetailsMRAY_1 MraY family signature 1. KkyTPTMGGIvIL
ChainResidueDetails
ALYS70-LEU82
site_idPS01348
Number of Residues12
DetailsMRAY_2 MraY family signature 2. NavNlTDGLDGL
ChainResidueDetails
AASN187-LEU198
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues88
DetailsTransmembrane: {"description":"Helical; Name=Helix 1","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues68
DetailsTransmembrane: {"description":"Helical; Name=Helix 2","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues164
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Helix 3","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues97
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Helix 4","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Helix 5","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Helix 6","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Helix 7","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=Helix 8","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues75
DetailsTransmembrane: {"description":"Helical; Name=Helix 9","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues88
DetailsTransmembrane: {"description":"Helical; Name=Helix 10","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues33
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27088606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CKR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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