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4MRN

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 Residues9
DetailsBINDING SITE FOR RESIDUE LDA A 701
ChainResidue
ATHR113
ALEU116
AALA117
AARG146
AGLY147
ATHR148
AILE330
AASP331
AMSE335

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LDA A 702
ChainResidue
AASP217
ATYR247
BVAL120
BILE144
BLDA702

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 703
ChainResidue
AARG114
AHIS115
BARG252

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 704
ChainResidue
ASER396
AGLY399
ALYS400
ASER401
AHOH932

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 705
ChainResidue
AARG206
AARG210
ALEU265
AMSE320
AARG323

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LDA B 701
ChainResidue
AVAL120
ATHR148
BASP217
BTYR247
BTYR254

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE LDA B 702
ChainResidue
ALDA702
BTHR113
BALA117
BARG146
BGLY147
BTHR148
BILE151
BASP331
BGLU334
BMSE335
BHOH864

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 703
ChainResidue
BSER396
BGLY399
BLYS400
BSER401

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 704
ChainResidue
BARG114
BHIS115
BHOH827

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 705
ChainResidue
BARG206
BARG210
BARG323

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

245663

PDB entries from 2025-12-03

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