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4MRP

Structure of a bacterial Atm1-family ABC transporter

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
B0000166molecular_functionnucleotide binding
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 Residues8
DetailsBINDING SITE FOR RESIDUE LDA A 701
ChainResidue
ATHR113
AARG146
AGLY147
ATHR148
AILE330
AASP331
AGLU334
AMSE335

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LDA A 702
ChainResidue
ATYR247
BALA117
BVAL120
BTHR148
AASP217

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GSH A 703
ChainResidue
AASN269
AGLN272
AASP316
AMSE317
ALEU318
AGLY319
AMSE320
BTYR156
BMSE317
BGSH703

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 704
ChainResidue
AARG114
AHOH870
BARG252

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 705
ChainResidue
APRO395
ASER396
AGLY397
AALA398
AGLY399
ALYS400
ASER401

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LDA B 701
ChainResidue
AALA117
AILE144
ATHR148
BASP217
BALA224
BTYR247

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LDA B 702
ChainResidue
BTHR113
BALA117
BARG146
BGLY147
BTHR148
BASP331
BGLU334
BMSE335

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GSH B 703
ChainResidue
ATYR156
AMSE317
AGSH703
BLEU268
BASN269
BGLN272
BASP316
BMSE317
BLEU318
BGLY319
BMSE320

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 704
ChainResidue
BSER396
BGLY399
BLYS400
BSER401
BHOH804

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 705
ChainResidue
AARG252
BARG114
BHIS115
BHOH888

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 Residues134
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues96
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MRP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9NP58","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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