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6VQT

Structure of a bacterial Atm1-family ABC exporter with MgADPVO4 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 Residues11
Detailsbinding site for residue ADP A 701
ChainResidue
ATYR370
BLYS497
BSER499
AARG374
ASER396
AGLY397
AGLY399
ALYS400
ASER401
AVO4702
AMG703

site_idAC2
Number of Residues11
Detailsbinding site for residue VO4 A 702
ChainResidue
ALYS400
ASER401
AGLN442
AGLU523
AHIS554
AADP701
AMG703
BSER499
BGLY500
BGLY501
BALA527

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 703
ChainResidue
ASER401
AGLN442
AADP701
AVO4702

site_idAC4
Number of Residues10
Detailsbinding site for residue VO4 A 704
ChainResidue
ASER499
AGLY500
AALA527
BGLY397
BLYS400
BGLN442
BGLU523
BHIS554
BADP701
BMG702

site_idAC5
Number of Residues12
Detailsbinding site for residue ADP B 701
ChainResidue
ALYS497
ASER499
AVO4704
BTYR370
BARG374
BGLY397
BALA398
BGLY399
BLYS400
BSER401
BTHR402
BMG702

site_idAC6
Number of Residues5
Detailsbinding site for residue MG B 702
ChainResidue
ASER499
AVO4704
BSER401
BGLN442
BADP701

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
AMET1-ARG38
AGLU106-MET154
ATHR203-GLY266
AARG323-GLU608
BMET1-ARG38
BGLU106-MET154
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

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PDB entries from 2024-05-01

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