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7Y48

Cryo-EM Structure of biliverdin-bound mitochondrial ABC transporter ABCB10 from Biortus

Functional Information from GO Data
ChainGOidnamespacecontents
B0005524molecular_functionATP binding
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
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. LSGGQKQRIAIARAL
ChainResidueDetails
BLEU634-LEU648

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues100
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BLEU171-PHE191
BLEU216-MET236
BASN313-GLY333
BLEU408-VAL428
BLEU431-PHE451

site_idSWS_FT_FI2
Number of Residues382
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000255
ChainResidueDetails
BLEU192-CYS215
BARG334-ASN407
BTYR452-ALA738

site_idSWS_FT_FI3
Number of Residues76
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000255
ChainResidueDetails
BGLN237-PRO312
BGLY429-GLU430

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
BGLY527

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS265

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: S-glutathionyl cysteine => ECO:0000250|UniProtKB:Q9JI39
ChainResidueDetails
BCYS582

219869

PDB entries from 2024-05-15

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