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8J5Q

Cryo-EM structure of Mycobacterium tuberculosis OppABCD in the pre-translocation 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
D0015833biological_processpeptide transport
D0016020cellular_componentmembrane
D0016887molecular_functionATP hydrolysis activity
D0022857molecular_functiontransmembrane transporter activity
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 Residues25
DetailsBINDING: BINDING => ECO:0000269|PubMed:38548954, ECO:0007744|PDB:8J5T
ChainResidueDetails
DSER43
DARG147
DGLY158
DGLU159
DHIS213
DSER396
DGLY397
DSER398
DGLY399
DLYS400
DSER401
DGLY44
DTHR402
DGLN445
DARG495
DGLU499
DGLY503
DHIS558
DSER45
DGLY46
DLYS47
DSER48
DALA49
DTYR61
DGLN96

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:38548954, ECO:0007744|PDB:8J5Q, ECO:0007744|PDB:8J5R, ECO:0007744|PDB:8J5S, ECO:0007744|PDB:8J5T
ChainResidueDetails
DCYS286
DCYS292
DCYS299
DCYS317

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PDB entries from 2025-06-11

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