Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8J5R

Cryo-EM structure of Mycobacterium tuberculosis OppABCD in the resting state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0015031biological_processprotein transport
A0015833biological_processpeptide transport
A0017038biological_processprotein import
A0042277molecular_functionpeptide binding
A0042597cellular_componentperiplasmic space
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0043295molecular_functionglutathione binding
A0055085biological_processtransmembrane transport
A1904680molecular_functionpeptide transmembrane transporter activity
B0005886cellular_componentplasma membrane
B0015031biological_processprotein transport
B0015833biological_processpeptide transport
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0055085biological_processtransmembrane transport
C0005886cellular_componentplasma membrane
C0015031biological_processprotein transport
C0015640molecular_functionpeptidoglycan peptide transmembrane transporter activity
C0015833biological_processpeptide transport
C0015834biological_processpeptidoglycan-associated peptide transport
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
D0000166molecular_functionnucleotide binding
D0005524molecular_functionATP binding
D0005886cellular_componentplasma membrane
D0009274cellular_componentpeptidoglycan-based cell wall
D0015031biological_processprotein transport
D0015421molecular_functionABC-type oligopeptide transporter activity
D0015833biological_processpeptide transport
D0016887molecular_functionATP hydrolysis activity
D0022857molecular_functiontransmembrane transporter activity
D0035672biological_processoligopeptide transmembrane transport
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
D0055085biological_processtransmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGERQRVVIAIAI
ChainResidueDetails
DLEU155-ILE169
DPHE500-LEU514

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues239
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues399
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues250
DetailsDomain: {"description":"ABC transporter 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues250
DetailsDomain: {"description":"ABC transporter 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues25
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38548954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8J5T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38548954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8J5Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8J5R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8J5S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8J5T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

PDB statisticsPDBj update infoContact PDBjnumon