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2A27

Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 8 monomers in the asymmetric unit

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
F0004672molecular_functionprotein kinase activity
F0005524molecular_functionATP binding
F0006468biological_processprotein phosphorylation
G0004672molecular_functionprotein kinase activity
G0005524molecular_functionATP binding
G0006468biological_processprotein phosphorylation
H0004672molecular_functionprotein kinase activity
H0005524molecular_functionATP binding
H0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DTT A 1001
ChainResidue
APHE178
AGLY179
ALYS222
AHOH1018
EDTT1005

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DTT B 1002
ChainResidue
BPHE178
BGLY179
BHOH1051
CDTT1003

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DTT C 1003
ChainResidue
BDTT1002
CPHE178
CGLY179
CLYS222
CHOH1036
CHOH1043

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DTT E 1005
ChainResidue
ADTT1001
EPHE178
EGLY179
EHOH1007

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DTT D 1004
ChainResidue
DPHE178
DGLY179
DLYS222
DLEU226
DHOH1007
GDTT1006

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DTT G 1006
ChainResidue
DILE177
DDTT1004
GGLY179
GLYS222

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DTT F 1007
ChainResidue
FPHE178
FGLY179
FPRO181
FHOH1010
HILE177
HDTT1008

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DTT H 1008
ChainResidue
FILE177
FDTT1007
HPHE178
HGLY179

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAIVKkCrekstgleyaak......FIKK
ChainResidueDetails
ALEU19-LYS46

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML
ChainResidueDetails
AILE135-LEU147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP139
BASP139
CASP139
DASP139
EASP139
FASP139
GASP139
HASP139

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU19
BLEU19
CLEU19
DLEU19
ELEU19
FLEU19
GLEU19
HLEU19

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:10376525, ECO:0000269|PubMed:10629061
ChainResidueDetails
ALYS42
BLYS42
CLYS42
DLYS42
ELYS42
FLYS42
GLYS42
HLYS42

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER289
BSER289
CSER289
DSER289
ESER289
FSER289
GSER289
HSER289

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11230133
ChainResidueDetails
AALA308
BALA308
CALA308
DALA308
EALA308
FALA308
GALA308
HALA308

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLU143
AASP139

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP139
BLYS141

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP139
CLYS141

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP139
DLYS141

site_idCSA13
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASP139
ELYS141

site_idCSA14
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FASP139
FLYS141

site_idCSA15
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
GASP139
GLYS141

site_idCSA16
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
HASP139
HLYS141

site_idCSA17
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR180
AASP139
ALYS141

site_idCSA18
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR180
BASP139
BLYS141

site_idCSA19
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CTHR180
CASP139
CLYS141

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BGLU143
BASP139

site_idCSA20
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DTHR180
DASP139
DLYS141

site_idCSA21
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ETHR180
EASP139
ELYS141

site_idCSA22
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FTHR180
FASP139
FLYS141

site_idCSA23
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
GTHR180
GASP139
GLYS141

site_idCSA24
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
HTHR180
HASP139
HLYS141

site_idCSA25
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP139
ALYS141
AASN144

site_idCSA26
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP139
BLYS141
BASN144

site_idCSA27
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP139
CLYS141
CASN144

site_idCSA28
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP139
DLYS141
DASN144

site_idCSA29
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASP139
ELYS141
EASN144

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CGLU143
CASP139

site_idCSA30
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FASP139
FLYS141
FASN144

site_idCSA31
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
GASP139
GLYS141
GASN144

site_idCSA32
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
HASP139
HLYS141
HASN144

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DGLU143
DASP139

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EGLU143
EASP139

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
FGLU143
FASP139

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
GGLU143
GASP139

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
HGLU143
HASP139

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP139
ALYS141

237735

PDB entries from 2025-06-18

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