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6OQQ

Legionella pneumophila SidJ/Saccharomyces cerevisiae calmodulin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0006508biological_processproteolysis
A0008152biological_processmetabolic process
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
B0000131cellular_componentincipient cellular bud site
B0000742biological_processkaryogamy involved in conjugation with cellular fusion
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005816cellular_componentspindle pole body
B0005823cellular_componentcentral plaque of spindle pole body
B0005856cellular_componentcytoskeleton
B0005933cellular_componentcellular bud
B0005934cellular_componentcellular bud tip
B0005935cellular_componentcellular bud neck
B0006606biological_processprotein import into nucleus
B0006661biological_processphosphatidylinositol biosynthetic process
B0006897biological_processendocytosis
B0006898biological_processreceptor-mediated endocytosis
B0007010biological_processcytoskeleton organization
B0007114biological_processcell budding
B0010968biological_processregulation of microtubule nucleation
B0016237biological_processmicroautophagy
B0016460cellular_componentmyosin II complex
B0030050biological_processvesicle transport along actin filament
B0030234molecular_functionenzyme regulator activity
B0030479cellular_componentactin cortical patch
B0031475cellular_componentmyosin V complex
B0042144biological_processvacuole fusion, non-autophagic
B0043332cellular_componentmating projection tip
B0045160cellular_componentmyosin I complex
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0051019molecular_functionmitogen-activated protein kinase binding
B0051300biological_processspindle pole body organization
B1903525biological_processregulation of membrane tubulation
B2000601biological_processpositive regulation of Arp2/3 complex-mediated actin nucleation
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0006508biological_processproteolysis
C0008152biological_processmetabolic process
C0008233molecular_functionpeptidase activity
C0008234molecular_functioncysteine-type peptidase activity
C0016740molecular_functiontransferase activity
C0016787molecular_functionhydrolase activity
C0016874molecular_functionligase activity
C0046872molecular_functionmetal ion binding
D0000131cellular_componentincipient cellular bud site
D0000742biological_processkaryogamy involved in conjugation with cellular fusion
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005816cellular_componentspindle pole body
D0005823cellular_componentcentral plaque of spindle pole body
D0005856cellular_componentcytoskeleton
D0005933cellular_componentcellular bud
D0005934cellular_componentcellular bud tip
D0005935cellular_componentcellular bud neck
D0006606biological_processprotein import into nucleus
D0006661biological_processphosphatidylinositol biosynthetic process
D0006897biological_processendocytosis
D0006898biological_processreceptor-mediated endocytosis
D0007010biological_processcytoskeleton organization
D0007114biological_processcell budding
D0010968biological_processregulation of microtubule nucleation
D0016237biological_processmicroautophagy
D0016460cellular_componentmyosin II complex
D0030050biological_processvesicle transport along actin filament
D0030234molecular_functionenzyme regulator activity
D0030479cellular_componentactin cortical patch
D0031475cellular_componentmyosin V complex
D0042144biological_processvacuole fusion, non-autophagic
D0043332cellular_componentmating projection tip
D0045160cellular_componentmyosin I complex
D0046872molecular_functionmetal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0051019molecular_functionmitogen-activated protein kinase binding
D0051300biological_processspindle pole body organization
D1903525biological_processregulation of membrane tubulation
D2000601biological_processpositive regulation of Arp2/3 complex-mediated actin nucleation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue AMP A 901
ChainResidue
AHIS492
AASN733
AHOH1257
AARG500
AASP502
AARG505
ATYR506
AGLN507
AGLN517
AGLN519
AGLY521

site_idAC2
Number of Residues11
Detailsbinding site for residue POP A 902
ChainResidue
AARG352
ALYS367
ALYS370
AASN534
AARG536
AASP542
AMG903
AMG904
AMG905
AHOH1033
AHOH1160

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 903
ChainResidue
AASP542
AASP545
APOP902

site_idAC4
Number of Residues3
Detailsbinding site for residue MG A 904
ChainResidue
ATYR449
AARG536
APOP902

site_idAC5
Number of Residues4
Detailsbinding site for residue MG A 905
ChainResidue
AGLN350
ATYR452
AARG536
APOP902

site_idAC6
Number of Residues1
Detailsbinding site for residue MG A 906
ChainResidue
ATHR493

site_idAC7
Number of Residues3
Detailsbinding site for residue NA A 907
ChainResidue
AARG522
AASN733
AHOH1043

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO A 908
ChainResidue
ALEU478
AARG479
ATYR599
AHOH1022
AHOH1037

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO A 909
ChainResidue
APHE563
ALEU598
AASN601
ATHR602
AGLU605

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO A 910
ChainResidue
ALEU694
AGLN695
AGLN698
AGLU707
AHOH1343

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO A 911
ChainResidue
ALYS666
AGLN667
AALA669
AASN670

site_idAD3
Number of Residues4
Detailsbinding site for residue EDO A 912
ChainResidue
AARG636
AILE671
AGLU672
AHOH1142

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO A 913
ChainResidue
AGLU637
AASN640
ATHR644

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO A 914
ChainResidue
ALYS219
AHIS226
AHIS280
ALEU792
AASP793

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO A 915
ChainResidue
AARG262
APHE292
AGLU294
CARG295

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO A 916
ChainResidue
ATHR574
APHE575
AHOH1118

site_idAD8
Number of Residues5
Detailsbinding site for residue CA B 201
ChainResidue
BASP21
BASP23
BASN25
BSER27
BHOH321

site_idAD9
Number of Residues4
Detailsbinding site for residue CA B 202
ChainResidue
BASP94
BASN96
BASP98
BLEU100

site_idAE1
Number of Residues4
Detailsbinding site for residue NA B 203
ChainResidue
BALA18
BASP21
BASN24
BHOH330

site_idAE2
Number of Residues14
Detailsbinding site for residue AMP C 901
ChainResidue
CHOH1133
CHOH1180
CHIS492
CARG500
CASP502
CARG505
CTYR506
CGLN507
CVAL510
CGLN517
CGLN519
CGLY521
CPOP903
CMG906

site_idAE3
Number of Residues10
Detailsbinding site for residue POP C 902
ChainResidue
CARG352
CLYS367
CARG536
CASP542
CMG904
CMG905
CHOH1003
CHOH1039
CHOH1062
CHOH1075

site_idAE4
Number of Residues8
Detailsbinding site for residue POP C 903
ChainResidue
CTHR493
CARG500
CTYR732
CASN733
CAMP901
CMG906
CHOH1011
CHOH1160

site_idAE5
Number of Residues4
Detailsbinding site for residue MG C 904
ChainResidue
CASP542
CASP545
CPOP902
CHOH1186

site_idAE6
Number of Residues2
Detailsbinding site for residue MG C 905
ChainResidue
CARG536
CPOP902

site_idAE7
Number of Residues3
Detailsbinding site for residue MG C 906
ChainResidue
CASN733
CAMP901
CPOP903

site_idAE8
Number of Residues5
Detailsbinding site for residue EDO C 907
ChainResidue
CLYS252
CTHR574
CPHE575
CHOH1048
CHOH1071

site_idAE9
Number of Residues6
Detailsbinding site for residue EDO C 908
ChainResidue
CLYS260
CSER303
CTHR304
CASP307
CGLN511
CHOH1037

site_idAF1
Number of Residues5
Detailsbinding site for residue EDO C 909
ChainResidue
CGLU284
CARG660
CTHR663
CPRO797
CGLY798

site_idAF2
Number of Residues5
Detailsbinding site for residue EDO C 910
ChainResidue
CLYS260
CSER585
CLEU586
CPHE587
CHOH1079

site_idAF3
Number of Residues4
Detailsbinding site for residue CA D 201
ChainResidue
DASP21
DASP23
DASN25
DSER27

site_idAF4
Number of Residues4
Detailsbinding site for residue CA D 202
ChainResidue
DASP94
DASN96
DASP98
DLEU100

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDNNGSISssEL
ChainResidueDetails
BASP21-LEU33
BASP57-PHE69
BASP94-LEU106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
BASP21
BGLU68
BASP94
BASN96
BASP98
BGLU105
DASP21
DASP23
DASN25
DSER27
DGLU32
BASP23
DASP57
DASP59
DASN61
DGLN63
DGLU68
DASP94
DASN96
DASP98
DGLU105
BASN25
BSER27
BGLU32
BASP57
BASP59
BASN61
BGLN63

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
BSER82
DSER82

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
BSER102
DSER102

218853

PDB entries from 2024-04-24

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