Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6HZM

Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005654cellular_componentnucleoplasm
A0005739cellular_componentmitochondrion
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0008514molecular_functionorganic anion transmembrane transporter activity
A0008559molecular_functionABC-type xenobiotic transporter activity
A0015143molecular_functionurate transmembrane transporter activity
A0015225molecular_functionbiotin transmembrane transporter activity
A0015562molecular_functionefflux transmembrane transporter activity
A0015711biological_processorganic anion transport
A0015747biological_processurate transport
A0015878biological_processbiotin transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0030148biological_processsphingolipid biosynthetic process
A0031526cellular_componentbrush border membrane
A0031966cellular_componentmitochondrial membrane
A0032217molecular_functionriboflavin transmembrane transporter activity
A0032218biological_processriboflavin transport
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0045121cellular_componentmembrane raft
A0046415biological_processurate metabolic process
A0046624molecular_functionsphingolipid transporter activity
A0046983molecular_functionprotein dimerization activity
A0055085biological_processtransmembrane transport
A0070633biological_processtransepithelial transport
A0097744biological_processrenal urate salt excretion
A0098591cellular_componentexternal side of apical plasma membrane
A0140115biological_processexport across plasma membrane
A0140359molecular_functionABC-type transporter activity
A0150104biological_processtransport across blood-brain barrier
A1990748biological_processcellular detoxification
A1990962biological_processxenobiotic transport across blood-brain barrier
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005654cellular_componentnucleoplasm
B0005739cellular_componentmitochondrion
B0005886cellular_componentplasma membrane
B0006869biological_processlipid transport
B0008514molecular_functionorganic anion transmembrane transporter activity
B0008559molecular_functionABC-type xenobiotic transporter activity
B0015143molecular_functionurate transmembrane transporter activity
B0015225molecular_functionbiotin transmembrane transporter activity
B0015562molecular_functionefflux transmembrane transporter activity
B0015711biological_processorganic anion transport
B0015747biological_processurate transport
B0015878biological_processbiotin transport
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0016887molecular_functionATP hydrolysis activity
B0030148biological_processsphingolipid biosynthetic process
B0031526cellular_componentbrush border membrane
B0031966cellular_componentmitochondrial membrane
B0032217molecular_functionriboflavin transmembrane transporter activity
B0032218biological_processriboflavin transport
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042910molecular_functionxenobiotic transmembrane transporter activity
B0045121cellular_componentmembrane raft
B0046415biological_processurate metabolic process
B0046624molecular_functionsphingolipid transporter activity
B0046983molecular_functionprotein dimerization activity
B0055085biological_processtransmembrane transport
B0070633biological_processtransepithelial transport
B0097744biological_processrenal urate salt excretion
B0098591cellular_componentexternal side of apical plasma membrane
B0140115biological_processexport across plasma membrane
B0140359molecular_functionABC-type transporter activity
B0150104biological_processtransport across blood-brain barrier
B1990748biological_processcellular detoxification
B1990962biological_processxenobiotic transport across blood-brain barrier
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue ATP A 1501
ChainResidue
AVAL46
ASER87
ASER88
AGLN126
AGLN211
AHIS243
AMG1502
AHOH1602
BLYS172
BARG184
BGLY185
ALEU48
BSER187
BGLY188
BGLY189
BGLU190
ALYS61
AILE63
ATHR82
AGLY83
AGLY84
AGLY85
ALYS86

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 1502
ChainResidue
ASER87
AGLN126
AGLN211
AATP1501
AHOH1602

site_idAC3
Number of Residues23
Detailsbinding site for residue ATP B 1501
ChainResidue
ALYS172
AARG184
AGLY185
ASER187
AGLY188
AGLY189
AGLU190
BVAL46
BLEU48
BLYS61
BILE63
BTHR82
BGLY83
BGLY84
BGLY85
BLYS86
BSER87
BSER88
BGLN126
BGLN211
BHIS243
BMG1502
BHOH1602

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 1502
ChainResidue
BSER87
BGLN126
BGLN211
BATP1501
BHOH1602

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues862
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-SER395
AVAL450-ASP477
AALA528-SER535
ALYS652-SER655
BMET1-SER395
BVAL450-ASP477
BALA528-SER535
BLYS652-SER655

site_idSWS_FT_FI2
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AILE396-LEU416
AVAL429-VAL449
ALEU478-GLY498
APHE507-ILE527
AVAL536-VAL556
AVAL631-LEU651
BILE396-LEU416
BVAL429-VAL449
BLEU478-GLY498
BPHE507-ILE527
BVAL536-VAL556
BVAL631-LEU651

site_idSWS_FT_FI3
Number of Residues182
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ALYS417-GLY428
ALEU499-PHE506
AASN557-HIS630
BLYS417-GLY428
BLEU499-PHE506
BASN557-HIS630

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:30405239, ECO:0007744|PDB:6HBU, ECO:0007744|PDB:6HZM
ChainResidueDetails
AGLY80
BGLY80

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:30405239, ECO:0007744|PDB:6HBU, ECO:0007744|PDB:6HZM
ChainResidueDetails
AHIS243
BARG184
BGLN211
BHIS243
AARG184
AGLN211

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:15807535
ChainResidueDetails
AASN418
AASN557
BASN418
BASN557

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PIM1 => ECO:0000269|PubMed:18056989
ChainResidueDetails
ATHR362
BTHR362

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15807535, ECO:0000269|PubMed:28554189, ECO:0007744|PDB:5NJ3, ECO:0007744|PDB:5NJG
ChainResidueDetails
AASN596
BASN596

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon