Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7TW2

Cryo-EM structure of human band 3 dimer from red blood cell

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005452molecular_functionsolute:inorganic anion antiporter activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006820biological_processmonoatomic anion transport
A0006821biological_processchloride transport
A0006873biological_processintracellular monoatomic ion homeostasis
A0007596biological_processblood coagulation
A0008509molecular_functionmonoatomic anion transmembrane transporter activity
A0009898cellular_componentcytoplasmic side of plasma membrane
A0015106molecular_functionbicarbonate transmembrane transporter activity
A0015108molecular_functionchloride transmembrane transporter activity
A0015297molecular_functionantiporter activity
A0015701biological_processbicarbonate transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0017121biological_processplasma membrane phospholipid scrambling
A0030018cellular_componentZ disc
A0030492molecular_functionhemoglobin binding
A0030506molecular_functionankyrin binding
A0030863cellular_componentcortical cytoskeleton
A0035811biological_processnegative regulation of urine volume
A0042803molecular_functionprotein homodimerization activity
A0043495molecular_functionprotein-membrane adaptor activity
A0045852biological_processpH elevation
A0048821biological_processerythrocyte development
A0051453biological_processregulation of intracellular pH
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0072659biological_processprotein localization to plasma membrane
A0140900molecular_functionchloride:bicarbonate antiporter activity
A0170014cellular_componentankyrin-1 complex
A1902476biological_processchloride transmembrane transport
A1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
B0005452molecular_functionsolute:inorganic anion antiporter activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006820biological_processmonoatomic anion transport
B0006821biological_processchloride transport
B0006873biological_processintracellular monoatomic ion homeostasis
B0007596biological_processblood coagulation
B0008509molecular_functionmonoatomic anion transmembrane transporter activity
B0009898cellular_componentcytoplasmic side of plasma membrane
B0015106molecular_functionbicarbonate transmembrane transporter activity
B0015108molecular_functionchloride transmembrane transporter activity
B0015297molecular_functionantiporter activity
B0015701biological_processbicarbonate transport
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0017121biological_processplasma membrane phospholipid scrambling
B0030018cellular_componentZ disc
B0030492molecular_functionhemoglobin binding
B0030506molecular_functionankyrin binding
B0030863cellular_componentcortical cytoskeleton
B0035811biological_processnegative regulation of urine volume
B0042803molecular_functionprotein homodimerization activity
B0043495molecular_functionprotein-membrane adaptor activity
B0045852biological_processpH elevation
B0048821biological_processerythrocyte development
B0051453biological_processregulation of intracellular pH
B0055085biological_processtransmembrane transport
B0070062cellular_componentextracellular exosome
B0072562cellular_componentblood microparticle
B0072659biological_processprotein localization to plasma membrane
B0140900molecular_functionchloride:bicarbonate antiporter activity
B0170014cellular_componentankyrin-1 complex
B1902476biological_processchloride transmembrane transport
B1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
Functional Information from PROSITE/UniProt
site_idPS00219
Number of Residues12
DetailsANION_EXCHANGER_1 Anion exchangers family signature 1. FGGLVRDIRRRY
ChainResidueDetails
BPHE379-TYR390

site_idPS00220
Number of Residues15
DetailsANION_EXCHANGER_2 Anion exchangers family signature 2. FLISLIFIYETFsKL
ChainResidueDetails
BPHE526-LEU540

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1080
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26542571
ChainResidueDetails
BMET1-PRO403
AGLN457-LEU459
APHE507-ARG518
ALYS592-ARG602
ATHR685-SER700
ALEU738-ARG760
ASER801-GLY838
AARG870-VAL911
BGLN457-LEU459
BPHE507-ARG518
BLYS592-ARG602
BTHR685-SER700
BLEU738-ARG760
BSER801-GLY838
BARG870-VAL911
AMET1-PRO403

site_idSWS_FT_FI2
Number of Residues46
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BGLN404-LEU427
AGLN404-LEU427

site_idSWS_FT_FI3
Number of Residues164
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:26542571
ChainResidueDetails
BGLY428-MET435
BSER477-GLU485
BLYS542-THR570
BILE624-MET663
AGLY428-MET435
ASER477-GLU485
ALYS542-THR570
AILE624-MET663

site_idSWS_FT_FI4
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BGLY436-ALA456
AGLY436-ALA456

site_idSWS_FT_FI5
Number of Residues32
DetailsTRANSMEM: Discontinuously helical; Name=3 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BLEU460-PHE476
ALEU460-PHE476

site_idSWS_FT_FI6
Number of Residues40
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BTYR486-ALA506
ATYR486-ALA506

site_idSWS_FT_FI7
Number of Residues44
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BTYR519-ILE541
ATYR519-ILE541

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BALA571-PHE591
AALA571-PHE591

site_idSWS_FT_FI9
Number of Residues40
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BARG603-PHE623
AARG603-PHE623

site_idSWS_FT_FI10
Number of Residues40
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BMET664-ILE684
AMET664-ILE684

site_idSWS_FT_FI11
Number of Residues36
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BGLY701-PHE719
AGLY701-PHE719

site_idSWS_FT_FI12
Number of Residues34
DetailsTRANSMEM: Discontinuously helical; Name=10 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BGLY720-ALA737
AGLY720-ALA737

site_idSWS_FT_FI13
Number of Residues40
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BILE761-SER781
AILE761-SER781

site_idSWS_FT_FI14
Number of Residues36
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:26542571
ChainResidueDetails
BARG782-LEU800
AARG782-LEU800

site_idSWS_FT_FI15
Number of Residues60
DetailsINTRAMEM: Discontinuously helical => ECO:0000269|PubMed:26542571
ChainResidueDetails
BILE839-LEU869
AILE839-LEU869

site_idSWS_FT_FI16
Number of Residues2
DetailsSITE: Important for anion transport
ChainResidueDetails
BLYS590
ALYS590

site_idSWS_FT_FI17
Number of Residues2
DetailsSITE: Important for anion-proton cotransport
ChainResidueDetails
BGLU681
AGLU681

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:2790053, ECO:0000269|PubMed:701248
ChainResidueDetails
BMET1
AMET1

site_idSWS_FT_FI19
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:10942405, ECO:0000269|PubMed:1998697
ChainResidueDetails
BTYR8
BTYR21
ATYR8
ATYR21

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:1998697
ChainResidueDetails
BTYR46
ATYR46

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23562
ChainResidueDetails
BSER185
ASER185

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04919
ChainResidueDetails
BSER350
ASER350

site_idSWS_FT_FI23
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:10942405
ChainResidueDetails
BTYR359
BTYR904
ATYR359
ATYR904

site_idSWS_FT_FI24
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:1885574
ChainResidueDetails
BCYS843
ACYS843

site_idSWS_FT_FI25
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10861210, ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:35835865
ChainResidueDetails
BASN642
AASN642

227933

PDB entries from 2024-11-27

PDB statisticsPDBj update infoContact PDBjnumon