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

2ONJ

Structure of the multidrug ABC transporter Sav1866 from S. aureus in complex with AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0015421molecular_functionABC-type oligopeptide transporter activity
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0035672biological_processoligopeptide transmembrane transport
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0015421molecular_functionABC-type oligopeptide transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0035672biological_processoligopeptide transmembrane transport
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 900
ChainResidue
AGLY367
AGLU368
ATHR369
ASER524
AARG527

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 901
ChainResidue
BANP700
BHOH808
BSER381
BGLN422
BASP502
BGLU503

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 910
ChainResidue
BGLY367
BGLU368
BTHR369
BSER524
BARG527

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 911
ChainResidue
ASER381
AGLN422
AASP502
AGLU503
AANP701

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ANP B 700
ChainResidue
AVAL476
ALYS477
ASER479
AGLY480
AGLY481
AALA507
BTYR349
BILE356
BSER376
BGLY377
BGLY378
BGLY379
BLYS380
BSER381
BTHR382
BGLN422
BGLU503
BHIS534
BHOH808
BHOH809
BNA901

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ANP A 701
ChainResidue
ATYR349
AILE356
ASER376
AGLY377
AGLY378
AGLY379
ALYS380
ASER381
ATHR382
ATYR391
AGLN422
AGLU503
AHIS534
AHOH818
AHOH819
ANA911
BVAL476
BLYS477
BSER479
BGLY480
BGLY481

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRLSIARIF
ChainResidueDetails
ALEU478-PHE492

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues842
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues230
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues58
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues580
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues470
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

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon