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4YER

Crystal structure of an ABC transporter ATP-binding protein (TM_1403) from Thermotoga maritima MSB8 at 2.35 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
A0043215biological_processdaunorubicin transport
A1900753biological_processdoxorubicin transport
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
B0043215biological_processdaunorubicin transport
B1900753biological_processdoxorubicin transport
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ADP A 400
ChainResidue
APHE14
ATHR44
ATHR45
BTHR135
BPHE136
BSER137
APHE17
AALA19
APRO38
AASN39
AGLY40
AALA41
AGLY42
ALYS43

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 401
ChainResidue
AASP210
ALYS213
BLYS13

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 402
ChainResidue
AHIS194
AGLU308
BHIS194
BGLU308

site_idAC4
Number of Residues16
Detailsbinding site for residue ADP B 400
ChainResidue
ALYS134
ATHR135
APHE136
ASER137
BPHE14
BPHE17
BALA19
BPRO38
BASN39
BGLY40
BALA41
BGLY42
BLYS43
BTHR44
BTHR45
BHOH512

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. FSGGMARRLEIARSL
ChainResidueDetails
APHE136-LEU150

223166

PDB entries from 2024-07-31

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