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6K4R

Crystal structure of SidJ-CaM-AMP ternary complex at 3.11 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0016740molecular_functiontransferase activity
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
B0016740molecular_functiontransferase activity
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
C0000086biological_processG2/M transition of mitotic cell cycle
C0000922cellular_componentspindle pole
C0002027biological_processregulation of heart rate
C0005509molecular_functioncalcium ion binding
C0005513biological_processdetection of calcium ion
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005819cellular_componentspindle
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005876cellular_componentspindle microtubule
C0005886cellular_componentplasma membrane
C0007186biological_processG protein-coupled receptor signaling pathway
C0008076cellular_componentvoltage-gated potassium channel complex
C0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
C0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
C0010856molecular_functionadenylate cyclase activator activity
C0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
C0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
C0016020cellular_componentmembrane
C0016240biological_processautophagosome membrane docking
C0019855molecular_functioncalcium channel inhibitor activity
C0019901molecular_functionprotein kinase binding
C0021762biological_processsubstantia nigra development
C0030017cellular_componentsarcomere
C0031432molecular_functiontitin binding
C0031514cellular_componentmotile cilium
C0031954biological_processpositive regulation of protein autophosphorylation
C0031982cellular_componentvesicle
C0032465biological_processregulation of cytokinesis
C0032516biological_processpositive regulation of phosphoprotein phosphatase activity
C0032991cellular_componentprotein-containing complex
C0034704cellular_componentcalcium channel complex
C0035307biological_processpositive regulation of protein dephosphorylation
C0035458biological_processcellular response to interferon-beta
C0043209cellular_componentmyelin sheath
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0044325molecular_functiontransmembrane transporter binding
C0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
C0046872molecular_functionmetal ion binding
C0048306molecular_functioncalcium-dependent protein binding
C0050848biological_processregulation of calcium-mediated signaling
C0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
C0051592biological_processresponse to calcium ion
C0055117biological_processregulation of cardiac muscle contraction
C0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
C0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
C0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
C0071346biological_processcellular response to type II interferon
C0071902biological_processpositive regulation of protein serine/threonine kinase activity
C0072542molecular_functionprotein phosphatase activator activity
C0097225cellular_componentsperm midpiece
C0098901biological_processregulation of cardiac muscle cell action potential
C0140056biological_processorganelle localization by membrane tethering
C1901842biological_processnegative regulation of high voltage-gated calcium channel activity
C1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
C1902494cellular_componentcatalytic complex
C1905913biological_processnegative regulation of calcium ion export across plasma membrane
C1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
D0000086biological_processG2/M transition of mitotic cell cycle
D0000922cellular_componentspindle pole
D0002027biological_processregulation of heart rate
D0005509molecular_functioncalcium ion binding
D0005513biological_processdetection of calcium ion
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005819cellular_componentspindle
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005876cellular_componentspindle microtubule
D0005886cellular_componentplasma membrane
D0007186biological_processG protein-coupled receptor signaling pathway
D0008076cellular_componentvoltage-gated potassium channel complex
D0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
D0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
D0010856molecular_functionadenylate cyclase activator activity
D0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
D0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
D0016020cellular_componentmembrane
D0016240biological_processautophagosome membrane docking
D0019855molecular_functioncalcium channel inhibitor activity
D0019901molecular_functionprotein kinase binding
D0021762biological_processsubstantia nigra development
D0030017cellular_componentsarcomere
D0031432molecular_functiontitin binding
D0031514cellular_componentmotile cilium
D0031954biological_processpositive regulation of protein autophosphorylation
D0031982cellular_componentvesicle
D0032465biological_processregulation of cytokinesis
D0032516biological_processpositive regulation of phosphoprotein phosphatase activity
D0032991cellular_componentprotein-containing complex
D0034704cellular_componentcalcium channel complex
D0035307biological_processpositive regulation of protein dephosphorylation
D0035458biological_processcellular response to interferon-beta
D0043209cellular_componentmyelin sheath
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0044325molecular_functiontransmembrane transporter binding
D0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
D0046872molecular_functionmetal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0050848biological_processregulation of calcium-mediated signaling
D0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
D0051592biological_processresponse to calcium ion
D0055117biological_processregulation of cardiac muscle contraction
D0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
D0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
D0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
D0071346biological_processcellular response to type II interferon
D0071902biological_processpositive regulation of protein serine/threonine kinase activity
D0072542molecular_functionprotein phosphatase activator activity
D0097225cellular_componentsperm midpiece
D0098901biological_processregulation of cardiac muscle cell action potential
D0140056biological_processorganelle localization by membrane tethering
D1901842biological_processnegative regulation of high voltage-gated calcium channel activity
D1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
D1902494cellular_componentcatalytic complex
D1905913biological_processnegative regulation of calcium ion export across plasma membrane
D1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue AMP A 901
ChainResidue
AARG352
ALYS367
ATYR532
AASN534
AARG536
AASP542
AASP545

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 902
ChainResidue
ALYS260
APHE587

site_idAC3
Number of Residues7
Detailsbinding site for residue AMP B 901
ChainResidue
BARG352
BLYS367
BGLN486
BASN534
BARG536
BASP542
BASP545

site_idAC4
Number of Residues2
Detailsbinding site for residue CL B 904
ChainResidue
BLEU586
BPHE587

site_idAC5
Number of Residues4
Detailsbinding site for residue CL B 905
ChainResidue
BARG505
BASN601
BTHR602
BGLU605

site_idAC6
Number of Residues4
Detailsbinding site for residue CA C 201
ChainResidue
CASP21
CASP23
CASP25
CTHR27

site_idAC7
Number of Residues5
Detailsbinding site for residue CA D 201
ChainResidue
DASP21
DASP23
DTHR27
DILE28
DTHR29

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
CASP21-LEU33
CASP57-PHE69
CASP94-LEU106
CASP130-PHE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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
CASP21
CASP23
CGLU32
DASP21
DASP23
DASP25
DTHR27
DGLU32
DASP57
DASP59
DASN61
DTHR63
DGLU68
CASP57
CASP59
CASN61
CTHR63
CGLU68
CASP25
CTHR27

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
ChainResidueDetails
DASP94
DASP96
DASN98
DTYR100
DGLU105
DASP130
DASP132
DASP134
DGLN136
DGLU141
CASP94
CASP96
CASN98
CTYR100
CGLU105
CASP130
CASP132
CASP134
CGLN136
CGLU141

site_idSWS_FT_FI3
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
CALA2
DALA2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS22
DLYS22

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
CTHR45
DTHR45

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER82
DSER82

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS95
DLYS95

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
CTYR100
DTYR100

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CSER102
DSER102

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CTHR111
DTHR111

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
CLYS116
DLYS116

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
CTYR139
DTYR139

site_idSWS_FT_FI13
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
DLYS22
CLYS22

219140

PDB entries from 2024-05-01

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