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3JU5

Crystal Structure of Dimeric Arginine Kinase at 1.75-A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004054molecular_functionarginine kinase activity
A0004111molecular_functioncreatine kinase activity
A0005524molecular_functionATP binding
A0016301molecular_functionkinase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046314biological_processphosphocreatine biosynthetic process
B0003824molecular_functioncatalytic activity
B0004054molecular_functionarginine kinase activity
B0004111molecular_functioncreatine kinase activity
B0005524molecular_functionATP binding
B0016301molecular_functionkinase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0046314biological_processphosphocreatine biosynthetic process
C0003824molecular_functioncatalytic activity
C0004054molecular_functionarginine kinase activity
C0004111molecular_functioncreatine kinase activity
C0005524molecular_functionATP binding
C0016301molecular_functionkinase activity
C0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
C0046314biological_processphosphocreatine biosynthetic process
D0003824molecular_functioncatalytic activity
D0004054molecular_functionarginine kinase activity
D0004111molecular_functioncreatine kinase activity
D0005524molecular_functionATP binding
D0016301molecular_functionkinase activity
D0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
D0046314biological_processphosphocreatine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 371
ChainResidue
AALA2
AARG50
AHOH1139
BHOH1007

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 371
ChainResidue
CALA2
CARG50
CHOH414

Functional Information from PROSITE/UniProt
site_idPS00112
Number of Residues7
DetailsPHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.SNLGT
ChainResidueDetails
ACYS274-THR280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843
ChainResidueDetails
ASER118
BARG311
CSER118
CHIS181
CARG226
CARG283
CARG311
DSER118
DHIS181
DARG226
DARG283
AHIS181
DARG311
AARG226
AARG283
AARG311
BSER118
BHIS181
BARG226
BARG283

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU222
DGLU222
DCYS274
DGLU316
ACYS274
AGLU316
BGLU222
BCYS274
BGLU316
CGLU222
CCYS274
CGLU316

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
AARG226
AARG122
AGLU222
AARG283

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
BARG226
BARG122
BGLU222
BARG283

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
CARG226
CARG122
CGLU222
CARG283

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
DARG226
DARG122
DGLU222
DARG283

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PDB entries from 2024-07-24

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