Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ZE3

Crystal structure of the integral membrane diacylglycerol kinase - delta7

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004143molecular_functionATP-dependent diacylglycerol kinase activity
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006654biological_processphosphatidic acid biosynthetic process
A0008610biological_processlipid biosynthetic process
A0008654biological_processphospholipid biosynthetic process
A0009411biological_processresponse to UV
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004143molecular_functionATP-dependent diacylglycerol kinase activity
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006654biological_processphosphatidic acid biosynthetic process
B0008610biological_processlipid biosynthetic process
B0008654biological_processphospholipid biosynthetic process
B0009411biological_processresponse to UV
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
C0000166molecular_functionnucleotide binding
C0004143molecular_functionATP-dependent diacylglycerol kinase activity
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006629biological_processlipid metabolic process
C0006654biological_processphosphatidic acid biosynthetic process
C0008610biological_processlipid biosynthetic process
C0008654biological_processphospholipid biosynthetic process
C0009411biological_processresponse to UV
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016740molecular_functiontransferase activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
D0000166molecular_functionnucleotide binding
D0004143molecular_functionATP-dependent diacylglycerol kinase activity
D0005524molecular_functionATP binding
D0005886cellular_componentplasma membrane
D0006629biological_processlipid metabolic process
D0006654biological_processphosphatidic acid biosynthetic process
D0008610biological_processlipid biosynthetic process
D0008654biological_processphospholipid biosynthetic process
D0009411biological_processresponse to UV
D0016020cellular_componentmembrane
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
D0016740molecular_functiontransferase activity
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0004143molecular_functionATP-dependent diacylglycerol kinase activity
E0005524molecular_functionATP binding
E0005886cellular_componentplasma membrane
E0006629biological_processlipid metabolic process
E0006654biological_processphosphatidic acid biosynthetic process
E0008610biological_processlipid biosynthetic process
E0008654biological_processphospholipid biosynthetic process
E0009411biological_processresponse to UV
E0016020cellular_componentmembrane
E0016301molecular_functionkinase activity
E0016310biological_processphosphorylation
E0016740molecular_functiontransferase activity
E0042802molecular_functionidentical protein binding
E0046872molecular_functionmetal ion binding
F0000166molecular_functionnucleotide binding
F0004143molecular_functionATP-dependent diacylglycerol kinase activity
F0005524molecular_functionATP binding
F0005886cellular_componentplasma membrane
F0006629biological_processlipid metabolic process
F0006654biological_processphosphatidic acid biosynthetic process
F0008610biological_processlipid biosynthetic process
F0008654biological_processphospholipid biosynthetic process
F0009411biological_processresponse to UV
F0016020cellular_componentmembrane
F0016301molecular_functionkinase activity
F0016310biological_processphosphorylation
F0016740molecular_functiontransferase activity
F0042802molecular_functionidentical protein binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA F 1122
ChainResidue
DLEU64
DASP107
DHOH2044
FSER60
FLEU64
FHOH2024

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA E 1122
ChainResidue
EHOH2020
DSER60
ESER61
ETHR111

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1122
ChainResidue
DGLU28
DGLU76
DFLC1123
DACT1124

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FLC D 1123
ChainResidue
DGLU76
DZN1122
DACT1124
DHOH2048

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT D 1124
ChainResidue
DGLU28
DGLU69
DASN72
DSER73
DGLU76
DZN1122
DFLC1123
DHOH2047

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 78N B 1122
ChainResidue
AALA13
AALA14
ASER17
A78N1123
A78N1124
BSER98
BVAL101
BLEU102
BILE105
BILE110
B78N1123

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 78N B 1123
ChainResidue
AARG9
A78N1124
BGLU34
BVAL65
BGLU69
BALA108
BTRP112
BALA113
B78N1122

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 78M D 1125
ChainResidue
AGLN33
AGLU34
A78M1126
CTRP117
C78N1122
DTRP25
DALA29
DARG32
DGLN33
DVAL36
DHOH2017
DHOH2049

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 78N C 1122
ChainResidue
A78M1126
BALA46
BARG55
BHOH2010
CILE110
CILE114
CTRP117
CSER118
DGLN33
D78M1125

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 78N A 1122
ChainResidue
ATRP18
AARG22
ATRP25
AILE26
ALEU39
AMET63
AMET66

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 78M D 1126
ChainResidue
AALA30
APHE31
AGLU34
AGLU69
ALEU102
AILE105
AHOH2012
DARG22
DTRP25
DHOH2050

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 78M D 1127
ChainResidue
BTRP47
BHOH2006
BHOH2008
DLEU102
DVAL109
DALA113
DHOH2018
DHOH2043

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 78N C 1123
ChainResidue
ALEU40
ATRP47
A78M1126
CGLU34
CGLU69
CTRP112

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 78M D 1128
ChainResidue
ATRP117
BGLY35
BVAL36
DTRP47
DLEU48
DASP49
DPHE120

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 78N A 1123
ChainResidue
AVAL42
AALA46
AARG55
A78N1124
AHOH2016
B78N1122

site_idBC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 78N A 1124
ChainResidue
AVAL50
AASP51
AALA52
AARG55
A78N1123
BILE114
BTRP117
B78N1122
B78N1123

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 78M A 1125
ChainResidue
AILE110
ATRP117
DALA46
DTRP47
DARG55

site_idBC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 78M A 1126
ChainResidue
ACYS41
APHE120
AHOH2015
CLEU102
CILE105
C78N1122
C78N1123
DLEU39
D78M1125

Functional Information from PROSITE/UniProt
site_idPS01069
Number of Residues12
DetailsDAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD
ChainResidueDetails
AGLU69-ASP80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues174
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:8071224
ChainResidueDetails
AALA1-ALA30
BALA1-ALA30
CALA1-ALA30
DALA1-ALA30
EALA1-ALA30
FALA1-ALA30

site_idSWS_FT_FI2
Number of Residues198
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
ChainResidueDetails
APHE31-TRP47
AASP51-VAL68
BPHE31-TRP47
BASP51-VAL68
CPHE31-TRP47
CASP51-VAL68
DPHE31-TRP47
DASP51-VAL68
EPHE31-TRP47
EASP51-VAL68
FPHE31-TRP47
FASP51-VAL68

site_idSWS_FT_FI3
Number of Residues12
DetailsTOPO_DOM: Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
ChainResidueDetails
ALEU48-VAL50
BLEU48-VAL50
CLEU48-VAL50
DLEU48-VAL50
ELEU48-VAL50
FLEU48-VAL50

site_idSWS_FT_FI4
Number of Residues150
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:8071224
ChainResidueDetails
AGLU69-LYS94
BGLU69-LYS94
CGLU69-LYS94
DGLU69-LYS94
EGLU69-LYS94
FGLU69-LYS94

site_idSWS_FT_FI5
Number of Residues138
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:8071224
ChainResidueDetails
AASP95-SER118
BASP95-SER118
CASP95-SER118
DASP95-SER118
EASP95-SER118
FASP95-SER118

site_idSWS_FT_FI6
Number of Residues12
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
ChainResidueDetails
AHIS119-GLY121
BHIS119-GLY121
CHIS119-GLY121
DHIS119-GLY121
EHIS119-GLY121
FHIS119-GLY121

site_idSWS_FT_FI7
Number of Residues6
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:26673816
ChainResidueDetails
AGLU69
BGLU69
CGLU69
DGLU69
EGLU69
FGLU69

site_idSWS_FT_FI8
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538
ChainResidueDetails
AARG9
BARG9
CARG9
DARG9
EARG9
FARG9

site_idSWS_FT_FI9
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
ChainResidueDetails
AALA13
BALA13
CALA13
DALA13
EALA13
FALA13

site_idSWS_FT_FI10
Number of Residues30
DetailsBINDING: BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
ChainResidueDetails
BGLU28
BGLU76
BGLU85
BLYS94
CTYR16
CGLU28
CGLU76
CGLU85
CLYS94
DTYR16
DGLU28
DGLU76
DGLU85
DLYS94
ETYR16
EGLU28
EGLU76
EGLU85
ELYS94
FTYR16
FGLU28
FGLU76
FGLU85
FLYS94
ATYR16
AGLU28
AGLU76
AGLU85
ALYS94
BTYR16

site_idSWS_FT_FI11
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129
ChainResidueDetails
AARG22
BARG22
CARG22
DARG22
EARG22
FARG22

site_idSWS_FT_FI12
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
ChainResidueDetails
AALA30
BALA30
CALA30
DALA30
EALA30
FALA30

site_idSWS_FT_FI13
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
ChainResidueDetails
ATRP47
BTRP47
CTRP47
DTRP47
ETRP47
FTRP47

site_idSWS_FT_FI14
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
ChainResidueDetails
AARG55
BARG55
CARG55
DARG55
EARG55
FARG55

site_idSWS_FT_FI15
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
ChainResidueDetails
AGLU69
BGLU69
CGLU69
DGLU69
EGLU69
FGLU69

site_idSWS_FT_FI16
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
ChainResidueDetails
ASER98
BSER98
CSER98
DSER98
ESER98
FSER98

site_idSWS_FT_FI17
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
ChainResidueDetails
ATRP112
BTRP112
CTRP112
DTRP112
ETRP112
FTRP112

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon