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3B8E

Crystal structure of the sodium-potassium pump

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002028biological_processregulation of sodium ion transport
A0005215molecular_functiontransporter activity
A0005391molecular_functionP-type sodium:potassium-exchanging transporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0005890cellular_componentsodium:potassium-exchanging ATPase complex
A0006813biological_processpotassium ion transport
A0006814biological_processsodium ion transport
A0006883biological_processintracellular sodium ion homeostasis
A0008556molecular_functionP-type potassium transmembrane transporter activity
A0010248biological_processestablishment or maintenance of transmembrane electrochemical gradient
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0030007biological_processintracellular potassium ion homeostasis
A0030424cellular_componentaxon
A0030955molecular_functionpotassium ion binding
A0031402molecular_functionsodium ion binding
A0036376biological_processsodium ion export across plasma membrane
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0042995cellular_componentcell projection
A0046872molecular_functionmetal ion binding
A0051117molecular_functionATPase binding
A0055085biological_processtransmembrane transport
A0086009biological_processmembrane repolarization
A1902600biological_processproton transmembrane transport
A1990573biological_processpotassium ion import across plasma membrane
B0005890cellular_componentsodium:potassium-exchanging ATPase complex
B0006813biological_processpotassium ion transport
B0006814biological_processsodium ion transport
C0000166molecular_functionnucleotide binding
C0002028biological_processregulation of sodium ion transport
C0005215molecular_functiontransporter activity
C0005391molecular_functionP-type sodium:potassium-exchanging transporter activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0005890cellular_componentsodium:potassium-exchanging ATPase complex
C0006813biological_processpotassium ion transport
C0006814biological_processsodium ion transport
C0006883biological_processintracellular sodium ion homeostasis
C0008556molecular_functionP-type potassium transmembrane transporter activity
C0010248biological_processestablishment or maintenance of transmembrane electrochemical gradient
C0016020cellular_componentmembrane
C0016323cellular_componentbasolateral plasma membrane
C0016887molecular_functionATP hydrolysis activity
C0030007biological_processintracellular potassium ion homeostasis
C0030424cellular_componentaxon
C0030955molecular_functionpotassium ion binding
C0031402molecular_functionsodium ion binding
C0036376biological_processsodium ion export across plasma membrane
C0042383cellular_componentsarcolemma
C0042470cellular_componentmelanosome
C0042995cellular_componentcell projection
C0046872molecular_functionmetal ion binding
C0051117molecular_functionATPase binding
C0055085biological_processtransmembrane transport
C0086009biological_processmembrane repolarization
C1902600biological_processproton transmembrane transport
C1990573biological_processpotassium ion import across plasma membrane
D0005890cellular_componentsodium:potassium-exchanging ATPase complex
D0006813biological_processpotassium ion transport
D0006814biological_processsodium ion transport
G0016020cellular_componentmembrane
G0043269biological_processregulation of monoatomic ion transport
G0099106molecular_functionion channel regulator activity
H0016020cellular_componentmembrane
H0043269biological_processregulation of monoatomic ion transport
H0099106molecular_functionion channel regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2002
ChainResidue
AGLY213
AASP369
ATHR371
AASP710
AMF42001

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RB A 2003
ChainResidue
AASP804
ATHR772
ASER775
AASN776
AGLU779

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE RB A 2004
ChainResidue
AVAL322
AASN324
AVAL325
AGLU327
AASN776
AGLU779
AASP804

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE RB A 2005
ChainResidue
AASP740

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 2002
ChainResidue
CGLY213
CASP369
CTHR371
CASP710
CMF42001

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RB C 2003
ChainResidue
CTHR772
CSER775
CASN776
CGLU779
CASP804

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE RB C 2004
ChainResidue
CVAL322
CVAL325
CGLU327
CASN776
CGLU779
CASP804

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE RB C 2005
ChainResidue
CASP740

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MF4 A 2001
ChainResidue
ATHR212
AGLY213
AGLU214
AASP369
ALYS370
ATHR371
AVAL609
ATHR610
AGLY611
AASP612
ALYS691
AASN713
AMG2002

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MF4 C 2001
ChainResidue
CTHR212
CGLY213
CGLU214
CASP369
CLYS370
CTHR371
CVAL609
CTHR610
CGLY611
CASP612
CLYS691
CASN713
CMG2002

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PC1 B 1
ChainResidue
BTYR43

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PC1 C 1
ChainResidue
CGLY848
DTYR39
DTYR43

Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP369-THR375

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues54
DetailsTRANSMEM: Helical; Signal-anchor for type II membrane protein => ECO:0000255
ChainResidueDetails
BILE35-SER62
AALA984-ARG1004
CCYS86-LEU106
CSER130-ILE150
CILE287-LEU306
CGLY319-CYS336
CTYR771-ASN790
CLEU801-GLU821
CLEU842-VAL864
CVAL917-SER936
CGLY950-GLY968
DILE35-SER62
CALA984-ARG1004
AILE287-LEU306
AGLY319-CYS336
ATYR771-ASN790
ALEU801-GLU821
ALEU842-VAL864
AVAL917-SER936
AGLY950-GLY968

site_idSWS_FT_FI2
Number of Residues214
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AALA107-LEU129
CVAL969-CYS983
AGLU307-ILE318
AILE791-ILE800
AILE865-PHE916
AVAL969-CYS983
CALA107-LEU129
CGLU307-ILE318
CILE791-ILE800
CILE865-PHE916

site_idSWS_FT_FI3
Number of Residues1198
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET151-HIS286
ALEU337-ALA770
ASER822-GLN841
AVAL937-PHE949
CMET151-HIS286
CLEU337-ALA770
CSER822-GLN841
CVAL937-PHE949

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250
ChainResidueDetails
ALEU374
CLEU374

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AILE485
ASER715
ALYS719
CILE485
CSER715
CLYS719

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8VDN2
ChainResidueDetails
ALYS21
CLYS21

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06685
ChainResidueDetails
ALYS38
AHIS45
ALEU450
AGLN482
CLYS38
CHIS45
CLEU450
CGLN482

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8VDN2
ChainResidueDetails
AASN226
AMET666
AASP673
CASN226
CMET666
CASP673

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q8VDN2
ChainResidueDetails
ATHR258
CTHR258

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05023
ChainResidueDetails
AGLY540
CGLY540

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8VDN2
ChainResidueDetails
AHIS659
CHIS659

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P06685
ChainResidueDetails
AGLY941
CGLY941

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1su4
ChainResidueDetails
AASP369

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1su4
ChainResidueDetails
CASP369

225681

PDB entries from 2024-10-02

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