Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PAN

Structure of a bacterial Atm1-family ABC exporter with ATP bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0046689biological_processresponse to mercury ion
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0046689biological_processresponse to mercury ion
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ATP A 701
ChainResidue
ATYR370
ASER401
ATHR402
AHIS554
BPHE479
BLYS497
BSER499
BGLU502
AARG374
AILE376
APRO395
ASER396
AGLY397
AALA398
AGLY399
ALYS400

site_idAC2
Number of Residues19
Detailsbinding site for residue ATP B 701
ChainResidue
ALYS497
ASER499
AGLY500
AGLY501
AGLU502
AALA527
BLEU133
BTYR370
BARG374
BILE376
BSER396
BGLY397
BALA398
BGLY399
BLYS400
BSER401
BTHR402
BARG405
BHIS554

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKQRVAIARTL
ChainResidueDetails
ALEU498-LEU512

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues134
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues96
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MRP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9NP58","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon