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6HR1

Crystal structure of the YFPnano fusion protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000086biological_processG2/M transition of mitotic cell cycle
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
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005876cellular_componentspindle microtubule
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006091biological_processgeneration of precursor metabolites and energy
A0007186biological_processG protein-coupled receptor signaling pathway
A0007259biological_processcell surface receptor signaling pathway via JAK-STAT
A0008076cellular_componentvoltage-gated potassium channel complex
A0008218biological_processbioluminescence
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
A0016240biological_processautophagosome membrane docking
A0019855molecular_functioncalcium channel inhibitor activity
A0019901molecular_functionprotein kinase binding
A0021762biological_processsubstantia nigra development
A0030017cellular_componentsarcomere
A0030672cellular_componentsynaptic vesicle membrane
A0031432molecular_functiontitin binding
A0031514cellular_componentmotile cilium
A0031982cellular_componentvesicle
A0032465biological_processregulation of cytokinesis
A0032991cellular_componentprotein-containing complex
A0034704cellular_componentcalcium channel complex
A0035458biological_processcellular response to interferon-beta
A0042995cellular_componentcell projection
A0043209cellular_componentmyelin sheath
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0044305cellular_componentcalyx of Held
A0044325molecular_functiontransmembrane transporter binding
A0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
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
A0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
A0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
A0071346biological_processcellular response to type II interferon
A0072542molecular_functionprotein phosphatase activator activity
A0097225cellular_componentsperm midpiece
A0097720biological_processcalcineurin-mediated signaling
A0098901biological_processregulation of cardiac muscle cell action potential
A0099523cellular_componentpresynaptic cytosol
A0140056biological_processorganelle localization by membrane tethering
A0140238biological_processpresynaptic endocytosis
A0141110molecular_functiontransporter inhibitor activity
A1901842biological_processnegative regulation of high voltage-gated calcium channel 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
A1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
B0000086biological_processG2/M transition of mitotic cell cycle
B0000922cellular_componentspindle pole
B0002027biological_processregulation of heart rate
B0005246molecular_functioncalcium channel regulator activity
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005876cellular_componentspindle microtubule
B0005886cellular_componentplasma membrane
B0005929cellular_componentcilium
B0006091biological_processgeneration of precursor metabolites and energy
B0007186biological_processG protein-coupled receptor signaling pathway
B0007259biological_processcell surface receptor signaling pathway via JAK-STAT
B0008076cellular_componentvoltage-gated potassium channel complex
B0008218biological_processbioluminescence
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0016020cellular_componentmembrane
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0021762biological_processsubstantia nigra development
B0030017cellular_componentsarcomere
B0030672cellular_componentsynaptic vesicle membrane
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031982cellular_componentvesicle
B0032465biological_processregulation of cytokinesis
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035458biological_processcellular response to interferon-beta
B0042995cellular_componentcell projection
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0044305cellular_componentcalyx of Held
B0044325molecular_functiontransmembrane transporter binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050848biological_processregulation of calcium-mediated signaling
B0051592biological_processresponse to calcium ion
B0055117biological_processregulation of cardiac muscle contraction
B0060291biological_processlong-term synaptic potentiation
B0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
B0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
B0071346biological_processcellular response to type II interferon
B0072542molecular_functionprotein phosphatase activator activity
B0097225cellular_componentsperm midpiece
B0097720biological_processcalcineurin-mediated signaling
B0098901biological_processregulation of cardiac muscle cell action potential
B0099523cellular_componentpresynaptic cytosol
B0140056biological_processorganelle localization by membrane tethering
B0140238biological_processpresynaptic endocytosis
B0141110molecular_functiontransporter inhibitor activity
B1901842biological_processnegative regulation of high voltage-gated calcium channel activity
B1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
B1902494cellular_componentcatalytic complex
B1905913biological_processnegative regulation of calcium ion export across plasma membrane
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue TLA A 901
ChainResidue
AGLY24
AHIS25
ALYS26
AARG358
ALYS367
ALEU368
AHOH1024
AHOH1031
AHOH1063

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 902
ChainResidue
AASP272
AASP274
AASP276
ATHR278
AGLU283
AHOH1007

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 903
ChainResidue
AASP308
AASP310
AASN312
ATHR314
AGLU319
AHOH1003

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 904
ChainResidue
AASP381
AASP383
AASP385
AGLN387
AGLU392
AHOH1030

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 905
ChainResidue
AASP345
AASP347
AASN349
ATYR351
AGLU356
AHOH1102

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 906
ChainResidue
AARG109
AARG122
AGLU124

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO A 907
ChainResidue
ALYS107
ALYS126

site_idAC8
Number of Residues6
Detailsbinding site for residue GOL A 908
ChainResidue
ALYS-27
ALYS52
ASER269
AGLY365
ALYS367
AHOH1036

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL A 909
ChainResidue
ALYS101
AASP102
AVAL176
AGLN177
ALEU178
AHOH1132

site_idAD1
Number of Residues6
Detailsbinding site for residue GOL A 910
ChainResidue
AASN164
APHE165
ALYS166
AASP180
AHIS181
ATYR182

site_idAD2
Number of Residues6
Detailsbinding site for residue CA B 501
ChainResidue
BASP272
BASP274
BASP276
BTHR278
BGLU283
BHOH692

site_idAD3
Number of Residues6
Detailsbinding site for residue CA B 502
ChainResidue
BASP345
BASP347
BASN349
BTYR351
BGLU356
BHOH741

site_idAD4
Number of Residues6
Detailsbinding site for residue CA B 503
ChainResidue
BASP308
BASP310
BASN312
BTHR314
BGLU319
BHOH691

site_idAD5
Number of Residues6
Detailsbinding site for residue CA B 504
ChainResidue
BASP381
BASP383
BASP385
BGLN387
BGLU392
BHOH643

site_idAD6
Number of Residues3
Detailsbinding site for residue NA B 505
ChainResidue
BGLU111
BLYS113
BHOH735

site_idAD7
Number of Residues4
Detailsbinding site for residue NA B 506
ChainResidue
BLYS113
BGLU115
BARG122
BHOH748

site_idAD8
Number of Residues2
Detailsbinding site for residue EDO B 507
ChainResidue
BILE382
BGLN395

site_idAD9
Number of Residues3
Detailsbinding site for residue EDO B 508
ChainResidue
BARG109
BARG122
BGLU124

site_idAE1
Number of Residues1
Detailsbinding site for residue EDO B 509
ChainResidue
BLYS107

site_idAE2
Number of Residues3
Detailsbinding site for residue EDO B 510
ChainResidue
BSER2
BGLU5
BGLN80

site_idAE3
Number of Residues4
Detailsbinding site for residue EDO B 511
ChainResidue
BGLN184
BARG96
BTHR97
BTYR182

site_idAE4
Number of Residues2
Detailsbinding site for residue EDO B 512
ChainResidue
BGLU379
BHOH638

site_idAE5
Number of Residues3
Detailsbinding site for residue EDO B 513
ChainResidue
BARG338
BARG342
BHOH778

site_idAE6
Number of Residues5
Detailsbinding site for residue GOL B 514
ChainResidue
AASN149
ATYR151
ATYR200
BGLU142
BGLU172

site_idAE7
Number of Residues8
Detailsbinding site for residue GOL B 515
ChainResidue
BLYS101
BASP102
BASN135
BVAL176
BGLN177
BLEU178
BHOH641
BHOH680

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
AASP274-THR286
AASP310-THR322
AASP347-HIS359
AASP383-GLN395

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132
ChainResidueDetails
ALEU68
BLEU68

site_idSWS_FT_FI2
Number of Residues4
DetailsCROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132
ChainResidueDetails
ACR266
AGLN69
BCR266
BGLN69

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
ChainResidueDetails
AASP272
AGLU319
BASP272
BASP274
BASP276
BTHR278
BGLU283
BASP308
BASP310
BASN312
BTHR314
AASP274
BGLU319
AASP276
ATHR278
AGLU283
AASP308
AASP310
AASN312
ATHR314

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0000269|PubMed:29724949, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03, ECO:0007744|PDB:6CNN, ECO:0007744|PDB:6CNO
ChainResidueDetails
AASP345
BGLU356
AASP347
AASN349
ATYR351
AGLU356
BASP345
BASP347
BASN349
BTYR351

site_idSWS_FT_FI5
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
ChainResidueDetails
AASP381
BGLU392
AASP383
AASP385
AGLN387
AGLU392
BASP381
BASP383
BASP385
BGLN387

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA253
BALA253

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS273
BLYS273

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
ATHR296
BTHR296

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER333
BSER333

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS346
BLYS346

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR351
BTYR351

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER353
BSER353

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR362
BTHR362

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS367
BLYS367

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR390
BTYR390

site_idSWS_FT_FI16
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
ALYS273
BLYS273

237992

PDB entries from 2025-06-25

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