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8XOK

Cryo-EM structure of human ABCC4

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKARVNLARAV
ChainResidueDetails
ALEU535-VAL549
APHE1177-ILE1191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues280
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALEU93-LEU113
ALEU836-VAL856
AVAL858-LEU878
AALA954-LEU974
AGLY977-VAL997
AGLU1038-LEU1058
AALA136-PHE156
AGLN207-ALA227
ALEU228-LEU248
ASER328-ALA348
AVAL351-SER371
ALEU440-GLY460
AHIS710-LEU730
ALEU771-VAL791

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY445
AGLY1075

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR646

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR648

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER664
ASER668

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26721430
ChainResidueDetails
AASN746
AASN754

222926

PDB entries from 2024-07-24

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