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7NNP

Rb-loaded cryo-EM structure of the E1-ATP KdpFABC complex.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006813biological_processpotassium ion transport
A0008556molecular_functionP-type potassium transmembrane transporter activity
A0030955molecular_functionpotassium ion binding
A0031004cellular_componentpotassium ion-transporting ATPase complex
A0071805biological_processpotassium ion transmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
A1903103cellular_componentpotassium:proton antiporter complex
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005215molecular_functiontransporter activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006813biological_processpotassium ion transport
B0008556molecular_functionP-type potassium transmembrane transporter activity
B0015662molecular_functionP-type ion transporter activity
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0031004cellular_componentpotassium ion-transporting ATPase complex
B0046872molecular_functionmetal ion binding
B0071805biological_processpotassium ion transmembrane transport
B0098655biological_processmonoatomic cation transmembrane transport
B1903103cellular_componentpotassium:proton antiporter complex
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006813biological_processpotassium ion transport
C0008556molecular_functionP-type potassium transmembrane transporter activity
C0016020cellular_componentmembrane
C0031004cellular_componentpotassium ion-transporting ATPase complex
C0071805biological_processpotassium ion transmembrane transport
C0098655biological_processmonoatomic cation transmembrane transport
C1903103cellular_componentpotassium:proton antiporter complex
D0005886cellular_componentplasma membrane
D0006813biological_processpotassium ion transport
D0008556molecular_functionP-type potassium transmembrane transporter activity
D0031004cellular_componentpotassium ion-transporting ATPase complex
D0043462biological_processregulation of ATP-dependent activity
D0071805biological_processpotassium ion transmembrane transport
D0098655biological_processmonoatomic cation transmembrane transport
D1903103cellular_componentpotassium:proton antiporter complex
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTIT
ChainResidueDetails
BASP307-THR313

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378
ChainResidueDetails
CMET1-ARG5
BPHE81-THR222
BPRO264-SER574
BILE632-ASN653
AMET436-PRO479
AALA553-SER557

site_idSWS_FT_FI2
Number of Residues28
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0007744|PDB:5MRW, ECO:0007744|PDB:6HRA
ChainResidueDetails
CPRO6-PHE34
APRO525-VAL552
BALA62-ASN80
BILE223-PHE242
BVAL252-ILE263
BLEU575-PHE595
BPRO613-LEU631
BLEU654-VAL678
ALYS415-ALA435
APHE480-MET501

site_idSWS_FT_FI3
Number of Residues155
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378
ChainResidueDetails
CPRO35-GLU190
BSER243-SER251
BALA596-SER612
BCYS679-VAL682
AALA502-GLY524

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:1474895
ChainResidueDetails
BASP307

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00, ECO:0007744|PDB:2A29
ChainResidueDetails
BASP344
BPHE377
BLYS395

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:16354672, ECO:0007744|PDB:2A00
ChainResidueDetails
BGLU348

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00285
ChainResidueDetails
BASP518
BASP522

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378
ChainResidueDetails
BALA162

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PDB entries from 2024-11-06

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