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6PAM

Structure of a bacterial Atm1-family ABC transporter with MgADP 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
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0016887molecular_functionATP hydrolysis activity
C0042626molecular_functionATPase-coupled transmembrane transporter activity
C0046689biological_processresponse to mercury ion
C0055085biological_processtransmembrane transport
C0140359molecular_functionABC-type transporter activity
D0005524molecular_functionATP binding
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0016887molecular_functionATP hydrolysis activity
D0042626molecular_functionATPase-coupled transmembrane transporter activity
D0046689biological_processresponse to mercury ion
D0055085biological_processtransmembrane transport
D0140359molecular_functionABC-type transporter activity
E0005524molecular_functionATP binding
E0005886cellular_componentplasma membrane
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0016887molecular_functionATP hydrolysis activity
E0042626molecular_functionATPase-coupled transmembrane transporter activity
E0046689biological_processresponse to mercury ion
E0055085biological_processtransmembrane transport
E0140359molecular_functionABC-type transporter activity
F0005524molecular_functionATP binding
F0005886cellular_componentplasma membrane
F0006811biological_processmonoatomic ion transport
F0016020cellular_componentmembrane
F0016887molecular_functionATP hydrolysis activity
F0042626molecular_functionATPase-coupled transmembrane transporter activity
F0046689biological_processresponse to mercury ion
F0055085biological_processtransmembrane transport
F0140359molecular_functionABC-type transporter activity
G0005524molecular_functionATP binding
G0005886cellular_componentplasma membrane
G0006811biological_processmonoatomic ion transport
G0016020cellular_componentmembrane
G0016887molecular_functionATP hydrolysis activity
G0042626molecular_functionATPase-coupled transmembrane transporter activity
G0046689biological_processresponse to mercury ion
G0055085biological_processtransmembrane transport
G0140359molecular_functionABC-type transporter activity
H0005524molecular_functionATP binding
H0005886cellular_componentplasma membrane
H0006811biological_processmonoatomic ion transport
H0016020cellular_componentmembrane
H0016887molecular_functionATP hydrolysis activity
H0042626molecular_functionATPase-coupled transmembrane transporter activity
H0046689biological_processresponse to mercury ion
H0055085biological_processtransmembrane transport
H0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue ADP A 701
ChainResidue
AHIS132
AMG702
ATYR370
AARG374
AILE376
ASER396
AGLY399
ALYS400
ASER401
ATHR402

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 702
ChainResidue
ASER401
AASP522
AADP701

site_idAC3
Number of Residues11
Detailsbinding site for residue ADP B 701
ChainResidue
BTYR370
BARG374
BILE376
BPRO395
BGLY397
BALA398
BGLY399
BLYS400
BSER401
BTHR402
BMG702

site_idAC4
Number of Residues3
Detailsbinding site for residue MG B 702
ChainResidue
BSER401
BASP522
BADP701

site_idAC5
Number of Residues11
Detailsbinding site for residue ADP C 701
ChainResidue
CLEU133
CTYR370
CARG374
CILE376
CSER396
CGLY399
CLYS400
CSER401
CTHR402
CARG405
CMG702

site_idAC6
Number of Residues2
Detailsbinding site for residue MG C 702
ChainResidue
CSER401
CADP701

site_idAC7
Number of Residues8
Detailsbinding site for residue ADP D 701
ChainResidue
DTYR370
DILE376
DALA398
DGLY399
DLYS400
DSER401
DTHR402
DMG702

site_idAC8
Number of Residues3
Detailsbinding site for residue MG D 702
ChainResidue
DSER401
DASP522
DADP701

site_idAC9
Number of Residues12
Detailsbinding site for residue ADP E 701
ChainResidue
EHIS132
EARG135
ETYR370
EARG374
EGLY397
EALA398
EGLY399
ELYS400
ESER401
ETHR402
EARG405
EMG702

site_idAD1
Number of Residues3
Detailsbinding site for residue MG E 702
ChainResidue
ESER401
EASP522
EADP701

site_idAD2
Number of Residues11
Detailsbinding site for residue ADP F 701
ChainResidue
FHIS132
FTYR370
FARG374
FPRO395
FGLY397
FALA398
FGLY399
FLYS400
FSER401
FTHR402
FMG702

site_idAD3
Number of Residues3
Detailsbinding site for residue MG F 702
ChainResidue
FSER401
FASP522
FADP701

site_idAD4
Number of Residues10
Detailsbinding site for residue ADP G 701
ChainResidue
GTYR370
GARG374
GPRO395
GSER396
GGLY399
GLYS400
GSER401
GARG405
GHIS554
GMG702

site_idAD5
Number of Residues3
Detailsbinding site for residue MG G 702
ChainResidue
GGLN442
GGLU523
GADP701

site_idAD6
Number of Residues11
Detailsbinding site for residue ADP H 701
ChainResidue
HSER401
HTHR402
HARG405
HHIS554
HMG702
HTYR370
HARG374
HPRO395
HSER396
HGLY399
HLYS400

site_idAD7
Number of Residues4
Detailsbinding site for residue MG H 702
ChainResidue
HSER401
HGLN442
HASP522
HADP701

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 Residues3464
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24604198
ChainResidueDetails
AMET1-ARG38
CGLU106-MET154
CTHR203-GLY266
CARG323-GLU608
DMET1-ARG38
DGLU106-MET154
DTHR203-GLY266
DARG323-GLU608
EMET1-ARG38
EGLU106-MET154
ETHR203-GLY266
AGLU106-MET154
EARG323-GLU608
FMET1-ARG38
FGLU106-MET154
FTHR203-GLY266
FARG323-GLU608
GMET1-ARG38
GGLU106-MET154
GTHR203-GLY266
GARG323-GLU608
HMET1-ARG38
ATHR203-GLY266
HGLU106-MET154
HTHR203-GLY266
HARG323-GLU608
AARG323-GLU608
BMET1-ARG38
BGLU106-MET154
BTHR203-GLY266
BARG323-GLU608
CMET1-ARG38

site_idSWS_FT_FI2
Number of Residues1016
DetailsTRANSMEM: Helical
ChainResidueDetails
AVAL39-TYR60
BPHE180-ILE202
BLEU267-ALA285
BLEU301-TYR322
CVAL39-TYR60
CPHE83-PHE105
CLEU155-LEU178
CPHE180-ILE202
CLEU267-ALA285
CLEU301-TYR322
DVAL39-TYR60
APHE83-PHE105
DPHE83-PHE105
DLEU155-LEU178
DPHE180-ILE202
DLEU267-ALA285
DLEU301-TYR322
EVAL39-TYR60
EPHE83-PHE105
ELEU155-LEU178
EPHE180-ILE202
ELEU267-ALA285
ALEU155-LEU178
ELEU301-TYR322
FVAL39-TYR60
FPHE83-PHE105
FLEU155-LEU178
FPHE180-ILE202
FLEU267-ALA285
FLEU301-TYR322
GVAL39-TYR60
GPHE83-PHE105
GLEU155-LEU178
APHE180-ILE202
GPHE180-ILE202
GLEU267-ALA285
GLEU301-TYR322
HVAL39-TYR60
HPHE83-PHE105
HLEU155-LEU178
HPHE180-ILE202
HLEU267-ALA285
HLEU301-TYR322
ALEU267-ALA285
ALEU301-TYR322
BVAL39-TYR60
BPHE83-PHE105
BLEU155-LEU178

site_idSWS_FT_FI3
Number of Residues288
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:24604198
ChainResidueDetails
ALYS61-ALA82
DLYS61-ALA82
DASN179
DTRP286-ASP300
ELYS61-ALA82
EASN179
ETRP286-ASP300
FLYS61-ALA82
FASN179
FTRP286-ASP300
GLYS61-ALA82
AASN179
GASN179
GTRP286-ASP300
HLYS61-ALA82
HASN179
HTRP286-ASP300
ATRP286-ASP300
BLYS61-ALA82
BASN179
BTRP286-ASP300
CLYS61-ALA82
CASN179
CTRP286-ASP300

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P40416
ChainResidueDetails
AARG206
BARG206
CARG206
DARG206
EARG206
FARG206
GARG206
HARG206

site_idSWS_FT_FI5
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:24604198, ECO:0007744|PDB:4MRP
ChainResidueDetails
AASN269
EASP316
FASN269
FASP316
GASN269
GASP316
HASN269
HASP316
AASP316
BASN269
BASP316
CASN269
CASP316
DASN269
DASP316
EASN269

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9NP58
ChainResidueDetails
ATYR370
BTYR370
CTYR370
DTYR370
ETYR370
FTYR370
GTYR370
HTYR370

site_idSWS_FT_FI7
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY394
BGLY394
CGLY394
DGLY394
EGLY394
FGLY394
GGLY394
HGLY394

227344

PDB entries from 2024-11-13

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