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2HQW

Crystal Structure of Ca2+/Calmodulin bound to NMDA Receptor NR1C1 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000086biological_processG2/M transition of mitotic cell cycle
A0000922cellular_componentspindle pole
A0001975biological_processresponse to amphetamine
A0002027biological_processregulation of heart rate
A0005246molecular_functioncalcium channel regulator activity
A0005509molecular_functioncalcium ion binding
A0005513biological_processdetection of calcium ion
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005876cellular_componentspindle microtubule
A0005929cellular_componentcilium
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
A0030234molecular_functionenzyme regulator activity
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
A0042995cellular_componentcell projection
A0043209cellular_componentmyelin sheath
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0043548molecular_functionphosphatidylinositol 3-kinase binding
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
A0090150biological_processestablishment of protein localization to membrane
A0090151biological_processestablishment of protein localization to mitochondrial membrane
A0097225cellular_componentsperm midpiece
A0098901biological_processregulation of cardiac muscle cell action potential
A0140056biological_processorganelle localization by membrane tethering
A1900242biological_processregulation of synaptic vesicle endocytosis
A1902494cellular_componentcatalytic complex
A1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
A2000300biological_processregulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AASP20
AASP22
AASP24
ATHR26
AGLU31
AHOH1027

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
ATHR62
AGLU67
AHOH1050
AASP56
AASP58
AASN60

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AASP93
AASP95
AASN97
ATYR99
AGLU104
AHOH1010

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AASP129
AASP131
AASP133
AGLN135
AGLU140
AHOH1012

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
AASP20-LEU32
AASP56-PHE68
AASP93-LEU105
AASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:Q05586
ChainResidueDetails
AGLY25
AILE27
ALEU32
BSER889
BSER896

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:15936117
ChainResidueDetails
AGLY59
AGLY61
AILE63
APHE68
BSER890

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:11588171
ChainResidueDetails
AGLY96
AGLY98
AILE100
ALEU105
BSER897

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD
ChainResidueDetails
AILE130
AGLY132
AGLY134
AVAL136
APHE141

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.8
ChainResidueDetails
AASP2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AASP22

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717
ChainResidueDetails
AGLU45

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AGLU82

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AASP95

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
AILE100

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
AALA102

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AASN111

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALEU116

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AGLU139

site_idSWS_FT_FI15
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
AASP22

218500

PDB entries from 2024-04-17

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