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7WIW

Cryo-EM structure of Mycobacterium tuberculosis irtAB complexed with ATP in an occluded conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006879biological_processintracellular iron ion homeostasis
A0010106biological_processcellular response to iron ion starvation
A0015343molecular_functionsiderophore-iron transmembrane transporter activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016887molecular_functionATP hydrolysis activity
A0033214biological_processsiderophore-iron import into cell
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0044847biological_processiron acquisition from host
A0055085biological_processtransmembrane transport
A0071949molecular_functionFAD binding
A0140359molecular_functionABC-type transporter activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006879biological_processintracellular iron ion homeostasis
B0010106biological_processcellular response to iron ion starvation
B0015343molecular_functionsiderophore-iron transmembrane transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0033214biological_processsiderophore-iron import into cell
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0044847biological_processiron acquisition from host
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGERQRLTIARAI
ChainResidueDetails
ALEU746-ILE760
BLEU470-LEU484

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues113
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues564
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues468
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues29
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"19948799","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues117
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"19948799","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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