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6TQF

The structure of ABC transporter Rv1819c in AMP-PNP bound state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0052572biological_processresponse to host immune response
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005886cellular_componentplasma membrane
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0052572biological_processresponse to host immune response
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue LMT A 801
ChainResidue
ATRP12
ASER13
APHE16
AMET131

site_idAC2
Number of Residues4
Detailsbinding site for residue LMT A 802
ChainResidue
ATRP22
ALYS25
AILE226
AALA230

site_idAC3
Number of Residues5
Detailsbinding site for residue LMT A 803
ChainResidue
ASER64
AVAL65
ATRP68
ALMT804
AGLY61

site_idAC4
Number of Residues5
Detailsbinding site for residue LMT A 804
ChainResidue
ALEU38
AARG42
ATRP52
AVAL60
ALMT803

site_idAC5
Number of Residues4
Detailsbinding site for residue LMT A 805
ChainResidue
ALEU214
APHE384
ATYR388
AARG395

site_idAC6
Number of Residues3
Detailsbinding site for residue MG A 806
ChainResidue
ATHR467
AGLN498
AANP807

site_idAC7
Number of Residues13
Detailsbinding site for residue ANP A 807
ChainResidue
ASER462
AGLY463
AGLY465
ALYS466
ATHR467
ATHR468
AARG471
AGLN498
AHIS607
AMG806
BSER552
BGLY554
BGLU555

site_idAC8
Number of Residues4
Detailsbinding site for residue LMT B 801
ChainResidue
BTRP12
BSER13
BPHE16
BMET131

site_idAC9
Number of Residues4
Detailsbinding site for residue LMT B 802
ChainResidue
BTRP22
BLYS25
BILE226
BALA230

site_idAD1
Number of Residues5
Detailsbinding site for residue LMT B 803
ChainResidue
BGLY61
BSER64
BVAL65
BTRP68
BLMT804

site_idAD2
Number of Residues5
Detailsbinding site for residue LMT B 804
ChainResidue
BLEU38
BARG42
BTRP52
BVAL60
BLMT803

site_idAD3
Number of Residues4
Detailsbinding site for residue LMT B 805
ChainResidue
BLEU214
BPHE384
BTYR388
BARG395

site_idAD4
Number of Residues3
Detailsbinding site for residue MG B 806
ChainResidue
BTHR467
BGLN498
BANP807

site_idAD5
Number of Residues13
Detailsbinding site for residue ANP B 807
ChainResidue
ASER552
AGLY554
AGLU555
BSER462
BGLY463
BGLY465
BLYS466
BTHR467
BTHR468
BARG471
BGLN498
BHIS607
BMG806

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSPGEQQRVAFARIL
ChainResidueDetails
ALEU551-LEU565

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AVAL20-LEU40
BTHR213-TRP233
BALA249-GLY269
BILE332-ILE352
ATRP68-PHE88
APHE121-ALA141
ATHR213-TRP233
AALA249-GLY269
AILE332-ILE352
BVAL20-LEU40
BTRP68-PHE88
BPHE121-ALA141

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:32296172
ChainResidueDetails
ASER462
AGLN498
BSER462
BGLN498

221716

PDB entries from 2024-06-26

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