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4HEX

A novel conformation of calmodulin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000086biological_processG2/M transition of mitotic cell cycle
A0000922cellular_componentspindle pole
A0002027biological_processregulation of heart rate
A0005509molecular_functioncalcium ion binding
A0005513biological_processdetection of calcium ion
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005876cellular_componentspindle microtubule
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
A0016240biological_processautophagosome membrane docking
A0019855molecular_functioncalcium channel inhibitor activity
A0019901molecular_functionprotein kinase binding
A0019904molecular_functionprotein domain specific binding
A0030017cellular_componentsarcomere
A0030235molecular_functionnitric-oxide synthase regulator activity
A0030426cellular_componentgrowth cone
A0030672cellular_componentsynaptic vesicle membrane
A0031432molecular_functiontitin binding
A0031514cellular_componentmotile cilium
A0031800molecular_functiontype 3 metabotropic glutamate receptor binding
A0031966cellular_componentmitochondrial membrane
A0032465biological_processregulation of cytokinesis
A0032991cellular_componentprotein-containing complex
A0034704cellular_componentcalcium channel complex
A0035307biological_processpositive regulation of protein dephosphorylation
A0035458biological_processcellular response to interferon-beta
A0043209cellular_componentmyelin sheath
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0043548molecular_functionphosphatidylinositol 3-kinase binding
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
A0050998molecular_functionnitric-oxide synthase binding
A0051592biological_processresponse to calcium ion
A0055117biological_processregulation of cardiac muscle contraction
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
A0098901biological_processregulation of cardiac muscle cell action potential
A0140056biological_processorganelle localization by membrane tethering
A0140238biological_processpresynaptic endocytosis
A1902494cellular_componentcatalytic complex
A1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
B0000086biological_processG2/M transition of mitotic cell cycle
B0000922cellular_componentspindle pole
B0002027biological_processregulation of heart rate
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005876cellular_componentspindle microtubule
B0008076cellular_componentvoltage-gated potassium channel complex
B0008179molecular_functionadenylate cyclase binding
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030017cellular_componentsarcomere
B0030235molecular_functionnitric-oxide synthase regulator activity
B0030426cellular_componentgrowth cone
B0030672cellular_componentsynaptic vesicle membrane
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031800molecular_functiontype 3 metabotropic glutamate receptor binding
B0031966cellular_componentmitochondrial membrane
B0032465biological_processregulation of cytokinesis
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035307biological_processpositive regulation of protein dephosphorylation
B0035458biological_processcellular response to interferon-beta
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0043548molecular_functionphosphatidylinositol 3-kinase binding
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
B0050998molecular_functionnitric-oxide synthase binding
B0051592biological_processresponse to calcium ion
B0055117biological_processregulation of cardiac muscle contraction
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
B0098901biological_processregulation of cardiac muscle cell action potential
B0140056biological_processorganelle localization by membrane tethering
B0140238biological_processpresynaptic endocytosis
B1902494cellular_componentcatalytic complex
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AASP57
AASP59
AASN61
ATHR63
AGLU68

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 202
ChainResidue
AGLU32
AASP21
AASP23
AASP25
ATHR27

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 203
ChainResidue
AASP94
AASP96
AASN98
ATYR100
AGLU105

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 204
ChainResidue
AASP130
AASP132
AASP134
AGLN136
AGLU141

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 205
ChainResidue
ATHR71
AASP81
AGLU85
BLYS95
BHIS108

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 201
ChainResidue
BASP130
BASP132
BASP134
BGLN136
BGLU141
BHOH322

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 202
ChainResidue
BASP94
BASP96
BASN98
BTYR100
BGLU105
BHOH305

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 203
ChainResidue
BASP57
BASP59
BASN61
BTHR63
BGLU68
BHOH332

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN B 204
ChainResidue
BASP21
BASP23
BASP25
BTHR27
BGLU32
BHOH307

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 205
ChainResidue
ALYS95
AHIS108
BTHR71
BASP81
BGLU85

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK
ChainResidueDetails
AASP21
AGLU68
AASP94
AASP96
AASN98
ATYR100
AGLU105
AASP130
AASP132
AASP134
AGLN136
AASP23
AGLU141
BASP21
BASP23
BASP25
BTHR27
BGLU32
BASP57
BASP59
BASN61
BTHR63
AASP25
BGLU68
BASP94
BASP96
BASN98
BTYR100
BGLU105
BASP130
BASP132
BASP134
BGLN136
ATHR27
BGLU141
AGLU32
AASP57
AASP59
AASN61
ATHR63

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.5
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS22
BLYS22

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
ATHR45
BTHR45

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ASER82
BSER82

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALYS95
BLYS95

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18034455, ECO:0007744|PubMed:21183079
ChainResidueDetails
ATYR100
BTYR100

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER102
BSER102

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ATHR111
BTHR111

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALYS116
BLYS116

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ATYR139
BTYR139

site_idSWS_FT_FI12
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
ALYS22
BLYS22

221716

PDB entries from 2024-06-26

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