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6J7M

Complex structure of the Pseudomonas aeruginosa rhamnosyltransferase EarP with the acceptor elongation factor EF-P

Functional Information from GO Data
ChainGOidnamespacecontents
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0106361molecular_functionprotein-arginine rhamnosyltransferase activity
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0106361molecular_functionprotein-arginine rhamnosyltransferase activity
M0003746molecular_functiontranslation elongation factor activity
M0005737cellular_componentcytoplasm
M0005829cellular_componentcytosol
M0006412biological_processtranslation
M0006414biological_processtranslational elongation
M0043043biological_processpeptide biosynthetic process
N0003746molecular_functiontranslation elongation factor activity
N0005737cellular_componentcytoplasm
N0005829cellular_componentcytosol
N0006412biological_processtranslation
N0006414biological_processtranslational elongation
N0043043biological_processpeptide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue TYD A 401
ChainResidue
AASN13
ATYR257
AARG270
AGLY271
AGLU272
AASP273
ASER274
AGOL402
ATYR14
AGLY15
AILE48
APHE190
ATYR192
APHE251
AMET252
AGLN254

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 402
ChainResidue
AASN13
ATYR192
AGLU272
ATYR290
ATYD401
MARG32
MHOH212

site_idAC3
Number of Residues16
Detailsbinding site for residue TYD C 401
ChainResidue
CASN13
CTYR14
CGLY15
CILE48
CPHE190
CTYR192
CPHE251
CMET252
CGLN254
CTYR257
CARG270
CGLY271
CGLU272
CASP273
CSER274
CGOL402

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL C 402
ChainResidue
CGLY15
CGLU272
CTYR290
CTYD401
CHOH603
NARG32

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"31010899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"31010899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31010899","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6J7K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31010899","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6J7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J7M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-alpha-linked (Rha) arginine","evidences":[{"source":"PubMed","id":"26060278","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28451135","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28451332","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31010899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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