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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9JUP

Structure of Arabidopsis thaliana ABCB1 with AMP-PNP bound in the outward-facing conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005783cellular_componentendoplasmic reticulum
A0005886cellular_componentplasma membrane
A0008361biological_processregulation of cell size
A0009506cellular_componentplasmodesma
A0009555biological_processpollen development
A0009624biological_processresponse to nematode
A0009637biological_processresponse to blue light
A0009639biological_processresponse to red or far red light
A0009640biological_processphotomorphogenesis
A0009733biological_processresponse to auxin
A0009734biological_processauxin-activated signaling pathway
A0009741biological_processresponse to brassinosteroid
A0009742biological_processbrassinosteroid mediated signaling pathway
A0009926biological_processauxin polar transport
A0009958biological_processpositive gravitropism
A0010315biological_processauxin export across the plasma membrane
A0010328molecular_functionauxin influx transmembrane transporter activity
A0010329molecular_functionauxin efflux transmembrane transporter activity
A0010928biological_processregulation of auxin mediated signaling pathway
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0043481biological_processanthocyanin accumulation in tissues in response to UV light
A0048229biological_processgametophyte development
A0048439biological_processflower morphogenesis
A0048443biological_processstamen development
A0048461biological_processflower structural organization
A0051510biological_processregulation of unidimensional cell growth
A0055085biological_processtransmembrane transport
A0060919biological_processauxin import into cell
A0090627biological_processplant epidermal cell differentiation
A0140359molecular_functionABC-type transporter activity
A1900459biological_processpositive regulation of brassinosteroid mediated signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRIAIARAM
ChainResidueDetails
ALEU507-MET521
ALEU1163-LEU1177
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. IGMTSGSSSrVK
ChainResidueDetails
AILE1271-LYS1282
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues244
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues288
DetailsDomain: {"description":"ABC transmembrane type-1 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"OCT-2024","submissionDatabase":"PDB data bank","title":"Structure of Arabidopsis thaliana ABCB1 with AMP-PNP bound in the inward-facing conformation under IAA condition.","authors":["Chen Q."]}},{"source":"PDB","id":"9JUK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"39497419","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2024","submissionDatabase":"PDB data bank","title":"Structure of Arabidopsis thaliana ABCB1 with AMP-PNP bound in the inward-facing conformation under IAA condition.","authors":["Chen Q."]}},{"source":"PDB","id":"8ZPZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8ZQ4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9JUL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9JUM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"39497419","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"OCT-2024","submissionDatabase":"PDB data bank","title":"Structure of Arabidopsis thaliana ABCB1 with AMP-PNP bound in the inward-facing conformation under IAA condition.","authors":["Chen Q."]}},{"source":"PDB","id":"8ZQ4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9JUK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"39497419","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8ZQ4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"39497419","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2024","submissionDatabase":"PDB data bank","title":"Structure of Arabidopsis thaliana ABCB1 with AMP-PNP bound in the inward-facing conformation under IAA condition.","authors":["Chen Q."]}},{"source":"PDB","id":"8ZPZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9JUL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9JUM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2024","submissionDatabase":"PDB data bank","title":"Structure of Arabidopsis thaliana ABCB1 with AMP-PNP bound in the inward-facing conformation under IAA condition.","authors":["Chen Q."]}},{"source":"PDB","id":"9JUL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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