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6QV0

Structure of ATP-bound outward-facing TM287/288 in complex with sybody Sb_TM35

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0016020cellular_componentmembrane
C0016887molecular_functionATP hydrolysis activity
C0042626molecular_functionATPase-coupled transmembrane transporter activity
C0046872molecular_functionmetal ion binding
C0055085biological_processtransmembrane transport
C0140359molecular_functionABC-type transporter activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005886cellular_componentplasma membrane
D0016020cellular_componentmembrane
D0016887molecular_functionATP hydrolysis activity
D0042626molecular_functionATPase-coupled transmembrane transporter activity
D0055085biological_processtransmembrane transport
D0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ATP A 600
ChainResidue
ATYR341
AGLN414
AMG601
BGLU490
BASP491
BLEU492
BSER493
BGLN494
BGLY495
BGLN496
AVAL348
ATHR368
AGLY369
ASER370
AGLY371
ALYS372
ASER373
ATHR374

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 601
ChainResidue
ASER373
AGLN414
AATP600

site_idAC3
Number of Residues21
Detailsbinding site for residue ATP B 600
ChainResidue
APHE451
AARG468
AASN469
ASER471
AGLY472
AGLY473
AGLN474
ASER499
BTYR364
BVAL370
BTHR390
BGLY391
BSER392
BGLY393
BLYS394
BTHR395
BTHR396
BTYR405
BGLN436
BHIS548
BMG601

site_idAC4
Number of Residues3
Detailsbinding site for residue MG B 601
ChainResidue
BTHR395
BGLN436
BATP600

site_idAC5
Number of Residues18
Detailsbinding site for residue ATP C 600
ChainResidue
CTYR341
CVAL348
CTHR368
CGLY369
CSER370
CGLY371
CLYS372
CSER373
CTHR374
CGLN414
CGLN526
CMG601
DASP491
DLEU492
DSER493
DGLY495
DGLN496
DASN521

site_idAC6
Number of Residues3
Detailsbinding site for residue MG C 601
ChainResidue
CSER373
CGLN414
CATP600

site_idAC7
Number of Residues21
Detailsbinding site for residue ATP D 600
ChainResidue
CPHE451
CARG468
CASN469
CSER471
CGLY472
CGLY473
CGLN474
CSER499
DTYR364
DVAL370
DTHR390
DGLY391
DSER392
DGLY393
DLYS394
DTHR395
DTHR396
DTYR405
DGLN436
DHIS548
DMG601

site_idAC8
Number of Residues3
Detailsbinding site for residue MG D 601
ChainResidue
DTHR395
DGLN436
DATP600

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. FSGGQKQRLSIARAL
ChainResidueDetails
APHE470-LEU484

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues200
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
BILE40-ILE60
DLEU273-VAL293
BMET80-ILE100
BVAL150-ILE170
BVAL177-VAL197
BLEU273-VAL293
DILE40-ILE60
DMET80-ILE100
DVAL150-ILE170
DVAL177-VAL197

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
BGLY388
DGLY388

226707

PDB entries from 2024-10-30

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