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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
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-dependent iron import into cell
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0044718biological_processsiderophore transmembrane transport
A0044847biological_processiron acquisition from host
A0055085biological_processtransmembrane transport
A0071949molecular_functionFAD binding
A0140359molecular_functionABC-type transporter activity
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-dependent iron import into cell
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0044718biological_processsiderophore transmembrane transport
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 Residues697
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:19948799
ChainResidueDetails
AMET1-PRO292
AHIS356-ALA408
AGLN454-ASP519
ALEU570-ARG859

site_idSWS_FT_FI2
Number of Residues120
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALEU293-LEU313
APHE335-LEU355
AVAL409-VAL429
AVAL433-ILE453
ALEU520-ALA540
ALEU549-GLY569

site_idSWS_FT_FI3
Number of Residues29
DetailsTOPO_DOM: Periplasmic => ECO:0000305|PubMed:19948799
ChainResidueDetails
ALEU314-GLY334
AASP430-ARG432
ATHR541-ASN548

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:G7CBF5
ChainResidueDetails
AARG70
AASP87
AALA97

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY643

219869

PDB entries from 2024-05-15

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