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5U6P

Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with cAMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005249molecular_functionvoltage-gated potassium channel activity
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005249molecular_functionvoltage-gated potassium channel activity
B0006811biological_processmonoatomic ion transport
B0006813biological_processpotassium ion transport
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005249molecular_functionvoltage-gated potassium channel activity
C0006811biological_processmonoatomic ion transport
C0006813biological_processpotassium ion transport
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005249molecular_functionvoltage-gated potassium channel activity
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue CMP A 901
ChainResidue
AMET530
AARG590
APHE538
AGLY539
AGLU540
AILE541
ACYS542
AARG549
ATHR550
AALA551

site_idAC2
Number of Residues10
Detailsbinding site for residue CMP B 901
ChainResidue
BMET530
BPHE538
BGLY539
BGLU540
BILE541
BCYS542
BARG549
BTHR550
BALA551
BARG590

site_idAC3
Number of Residues10
Detailsbinding site for residue CMP C 901
ChainResidue
CMET530
CPHE538
CGLY539
CGLU540
CILE541
CCYS542
CARG549
CTHR550
CALA551
CARG590

site_idAC4
Number of Residues10
Detailsbinding site for residue CMP D 901
ChainResidue
DMET530
DPHE538
DGLY539
DGLU540
DILE541
DCYS542
DARG549
DTHR550
DALA551
DARG590

Functional Information from PROSITE/UniProt
site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. IIrEGAvGKkMYFIqhG
ChainResidueDetails
AILE502-GLY518

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2684
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28086084
ChainResidueDetails
AMET1-ARG142
CARG195-MET215
CGLU282-VAL295
DMET1-ARG142
DARG195-MET215
DGLU282-VAL295
AARG195-MET215
AGLU282-VAL295
BMET1-ARG142
BARG195-MET215
BGLU282-VAL295
CMET1-ARG142

site_idSWS_FT_FI2
Number of Residues84
DetailsTRANSMEM: Helical; Name=Segment S1 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG
ChainResidueDetails
APHE143-ILE164
BPHE143-ILE164
CPHE143-ILE164
DPHE143-ILE164

site_idSWS_FT_FI3
Number of Residues240
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:28086084
ChainResidueDetails
ATHR165-THR173
CLEU237-THR260
CVAL319-GLN344
CVAL367-ASP371
DTHR165-THR173
DLEU237-THR260
DVAL319-GLN344
DVAL367-ASP371
ALEU237-THR260
AVAL319-GLN344
AVAL367-ASP371
BTHR165-THR173
BLEU237-THR260
BVAL319-GLN344
BVAL367-ASP371
CTHR165-THR173

site_idSWS_FT_FI4
Number of Residues80
DetailsTRANSMEM: Helical; Name=Segment S2 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG
ChainResidueDetails
APRO174-PHE194
BPRO174-PHE194
CPRO174-PHE194
DPRO174-PHE194

site_idSWS_FT_FI5
Number of Residues80
DetailsTRANSMEM: Helical; Name=Segment S3 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG
ChainResidueDetails
AASN216-PHE236
BASN216-PHE236
CASN216-PHE236
DASN216-PHE236

site_idSWS_FT_FI6
Number of Residues80
DetailsTRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG
ChainResidueDetails
ALYS261-TRP281
BLYS261-TRP281
CLYS261-TRP281
DLYS261-TRP281

site_idSWS_FT_FI7
Number of Residues88
DetailsTRANSMEM: Helical; Name=Segment S5 => ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG
ChainResidueDetails
AVAL296-LEU318
BVAL296-LEU318
CVAL296-LEU318
DVAL296-LEU318

site_idSWS_FT_FI8
Number of Residues84
DetailsINTRAMEM: Pore-forming; Name=Segment H5 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG
ChainResidueDetails
ATYR345-PRO366
BTYR345-PRO366
CTYR345-PRO366
DTYR345-PRO366

site_idSWS_FT_FI9
Number of Residues80
DetailsTRANSMEM: Helical; Name=Segment S6 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG
ChainResidueDetails
ALEU372-HIS392
BLEU372-HIS392
CLEU372-HIS392
DLEU372-HIS392

site_idSWS_FT_FI10
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:31787376, ECO:0000305|PubMed:28086084, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF
ChainResidueDetails
AGLY539
CCYS542
CARG549
CTHR550
DGLY539
DCYS542
DARG549
DTHR550
ACYS542
AARG549
ATHR550
BGLY539
BCYS542
BARG549
BTHR550
CGLY539

site_idSWS_FT_FI11
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:31787376, ECO:0007744|PDB:6UQF
ChainResidueDetails
AGLU540
AARG593
BGLU540
BARG593
CGLU540
CARG593
DGLU540
DARG593

site_idSWS_FT_FI12
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O88704
ChainResidueDetails
AARG590
BARG590
CARG590
DARG590

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN338
BASN338
CASN338
DASN338

222036

PDB entries from 2024-07-03

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