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8IPS

Cryo-EM structure of heme transporter CydDC from Escherichia coli in the inward facing heme loading state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006865biological_processamino acid transport
A0015439molecular_functionABC-type heme transporter activity
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0033228biological_processcysteine export across plasma membrane
A0034775biological_processglutathione transmembrane transport
A0035351biological_processheme transmembrane transport
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0045454biological_processcell redox homeostasis
A0055051cellular_componentATP-binding cassette (ABC) transporter complex, integrated substrate binding
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
A1903605biological_processcytochrome biosynthetic process
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006865biological_processamino acid transport
B0006869biological_processlipid transport
B0015439molecular_functionABC-type heme transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0033228biological_processcysteine export across plasma membrane
B0034040molecular_functionATPase-coupled lipid transmembrane transporter activity
B0034775biological_processglutathione transmembrane transport
B0035351biological_processheme transmembrane transport
B0042883biological_processcysteine transport
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0045454biological_processcell redox homeostasis
B0055051cellular_componentATP-binding cassette (ABC) transporter complex, integrated substrate binding
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
B1903605biological_processcytochrome biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGELRRLAIARAL
ChainResidueDetails
ALEU475-LEU489
BLEU486-LEU500

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues866
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15470119","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15470119","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues572
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues466
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

244693

PDB entries from 2025-11-12

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