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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6SZ5

Human calmodulin bound to a peptide of human NADPH oxidase 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000922cellular_componentspindle pole
A0002027biological_processregulation of heart rate
A0005246molecular_functioncalcium channel regulator activity
A0005509molecular_functioncalcium ion binding
A0005513biological_processdetection of calcium ion
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005876cellular_componentspindle microtubule
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0008076cellular_componentvoltage-gated potassium channel complex
A0008179molecular_functionadenylate cyclase binding
A0010856molecular_functionadenylate cyclase activator activity
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A0016020cellular_componentmembrane
A0019855molecular_functioncalcium channel inhibitor activity
A0019901molecular_functionprotein kinase binding
A0021762biological_processsubstantia nigra development
A0030017cellular_componentsarcomere
A0031432molecular_functiontitin binding
A0031982cellular_componentvesicle
A0032465biological_processregulation of cytokinesis
A0032991cellular_componentprotein-containing complex
A0034704cellular_componentcalcium channel complex
A0043209cellular_componentmyelin sheath
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0044305cellular_componentcalyx of Held
A0044325molecular_functiontransmembrane transporter binding
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0050848biological_processregulation of calcium-mediated signaling
A0051592biological_processresponse to calcium ion
A0055117biological_processregulation of cardiac muscle contraction
A0060291biological_processlong-term synaptic potentiation
A0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
A0072542molecular_functionprotein phosphatase activator activity
A0097225cellular_componentsperm midpiece
A0097720biological_processcalcineurin-mediated signaling
A0099523cellular_componentpresynaptic cytosol
A0140238biological_processpresynaptic endocytosis
A0141110molecular_functiontransporter inhibitor activity
A1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
A1902494cellular_componentcatalytic complex
A1905913biological_processnegative regulation of calcium ion export across plasma membrane
B0001525biological_processangiogenesis
B0001819biological_processpositive regulation of cytokine production
B0001935biological_processendothelial cell proliferation
B0005509molecular_functioncalcium ion binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006915biological_processapoptotic process
B0006952biological_processdefense response
B0015252molecular_functionproton channel activity
B0016175molecular_functionsuperoxide-generating NAD(P)H oxidase activity
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0034220biological_processmonoatomic ion transmembrane transport
B0042554biological_processsuperoxide anion generation
B0043012biological_processregulation of fusion of sperm to egg plasma membrane
B0043020cellular_componentNADPH oxidase complex
B0046872molecular_functionmetal ion binding
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
B0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
B0061640biological_processcytoskeleton-dependent cytokinesis
B0106292molecular_functionsuperoxide-generating NADPH oxidase activity
B1902600biological_processproton transmembrane transport
C0001525biological_processangiogenesis
C0001819biological_processpositive regulation of cytokine production
C0001935biological_processendothelial cell proliferation
C0005509molecular_functioncalcium ion binding
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006915biological_processapoptotic process
C0006952biological_processdefense response
C0015252molecular_functionproton channel activity
C0016175molecular_functionsuperoxide-generating NAD(P)H oxidase activity
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0034220biological_processmonoatomic ion transmembrane transport
C0042554biological_processsuperoxide anion generation
C0043012biological_processregulation of fusion of sperm to egg plasma membrane
C0043020cellular_componentNADPH oxidase complex
C0046872molecular_functionmetal ion binding
C0050660molecular_functionflavin adenine dinucleotide binding
C0050661molecular_functionNADP binding
C0050664molecular_functionoxidoreductase activity, acting on NAD(P)H, oxygen as acceptor
C0061640biological_processcytoskeleton-dependent cytokinesis
C0106292molecular_functionsuperoxide-generating NADPH oxidase activity
C1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA A 501
ChainResidue
AASP130
AASP132
AASP134
AGLN136
AGLU141
site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 502
ChainResidue
AGLU105
AASP94
AASP96
AASN98
ATYR100
site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 503
ChainResidue
AASP57
AASP59
AASN61
ATHR63
AGLU68
site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 504
ChainResidue
AASP21
AASP23
AASP25
ATHR27
AGLU32
AASP119
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
AASP21-LEU33
AASP57-PHE69
AASP94-LEU106
AASP130-PHE142
BASP25-LEU37
BASP61-LEU73
BASP105-LEU117
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP30","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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