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6PAQ

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

Functional Information from GO Data
ChainGOidnamespacecontents
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
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 Residues18
Detailsbinding site for residue ATP A 701
ChainResidue
ATYR370
ASER401
ATHR402
AARG405
AGLN442
AHIS554
BLYS497
BSER499
BGLY501
BGLU502
AASP371
AARG374
APRO395
ASER396
AGLY397
AALA398
AGLY399
ALYS400

site_idAC2
Number of Residues17
Detailsbinding site for residue ATP B 701
ChainResidue
ALYS497
ASER499
AGLY501
AALA527
BTYR370
BARG374
BILE376
BSER396
BGLY397
BALA398
BGLY399
BLYS400
BSER401
BTHR402
BARG405
BGLN442
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 Residues866
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24604198
ChainResidueDetails
AMSE1-ARG38
AGLU106-MSE154
ATHR203-GLY266
AARG323-GLU608
BMSE1-ARG38
BGLU106-MSE154
BTHR203-GLY266
BARG323-GLU608

site_idSWS_FT_FI2
Number of Residues254
DetailsTRANSMEM: Helical
ChainResidueDetails
AVAL39-TYR60
BPHE180-ILE202
BLEU267-ALA285
BLEU301-TYR322
APHE83-PHE105
ALEU155-LEU178
APHE180-ILE202
ALEU267-ALA285
ALEU301-TYR322
BVAL39-TYR60
BPHE83-PHE105
BLEU155-LEU178

site_idSWS_FT_FI3
Number of Residues72
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:24604198
ChainResidueDetails
ALYS61-ALA82
AASN179
ATRP286-ASP300
BLYS61-ALA82
BASN179
BTRP286-ASP300

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P40416
ChainResidueDetails
AARG206
BARG206

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:24604198, ECO:0007744|PDB:4MRP
ChainResidueDetails
AASN269
AASP316
BASN269
BASP316

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9NP58
ChainResidueDetails
ATYR370
BTYR370

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY394
BGLY394

220113

PDB entries from 2024-05-22

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