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

2HYD

Multidrug ABC transporter SAV1866

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
ATHR369
ASER524
ALYS525
AARG527

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 910
ChainResidue
BTHR529
BGLY367
BTHR369
BSER524
BARG527

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP A 700
ChainResidue
ATYR349
AILE356
ASER376
AGLY377
AGLY378
AGLY379
ALYS380
ASER381
ATHR382
ATYR391
AHOH802
BVAL476
BLYS477
BSER479

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP B 701
ChainResidue
ALEU463
AVAL476
ALYS477
ASER479
AGLN482
BTYR349
BILE356
BSER376
BGLY377
BGLY378
BGLY379
BLYS380
BSER381
BTHR382
BTYR391
BHOH812

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

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon