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8WAM

Cryo-EM structure of the ABCG25 E232Q mutant bound to ATP and Magnesium

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0009408biological_processresponse to heat
A0009409biological_processresponse to cold
A0009737biological_processresponse to abscisic acid
A0009738biological_processabscisic acid-activated signaling pathway
A0010496biological_processintercellular transport
A0015562molecular_functionefflux transmembrane transporter activity
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0048581biological_processnegative regulation of post-embryonic development
A0055085biological_processtransmembrane transport
A0080168biological_processabscisic acid transport
A0140352biological_processexport from cell
A0140359molecular_functionABC-type transporter activity
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0009408biological_processresponse to heat
B0009409biological_processresponse to cold
B0009737biological_processresponse to abscisic acid
B0009738biological_processabscisic acid-activated signaling pathway
B0010496biological_processintercellular transport
B0015562molecular_functionefflux transmembrane transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0048581biological_processnegative regulation of post-embryonic development
B0055085biological_processtransmembrane transport
B0080168biological_processabscisic acid transport
B0140352biological_processexport from cell
B0140359molecular_functionABC-type transporter activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues280
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AVAL374-LEU394
BLEU437-PHE457
BLEU489-LEU509
BVAL522-MET542
BALA547-ASN567
BVAL629-TYR649
APHE406-TRP426
ALEU437-PHE457
ALEU489-LEU509
AVAL522-MET542
AALA547-ASN567
AVAL629-TYR649
BVAL374-LEU394
BPHE406-TRP426

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY101
BGLY101

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN56
AASN122
BASN56
BASN122

221051

PDB entries from 2024-06-12

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