Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3JU6

Crystal Structure of Dimeric Arginine Kinase in Complex with AMPPNP and Arginine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004054molecular_functionarginine kinase activity
A0004111molecular_functioncreatine kinase activity
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046314biological_processphosphocreatine biosynthetic process
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004054molecular_functionarginine kinase activity
B0004111molecular_functioncreatine kinase activity
B0005524molecular_functionATP binding
B0005615cellular_componentextracellular space
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0046314biological_processphosphocreatine biosynthetic process
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004054molecular_functionarginine kinase activity
C0004111molecular_functioncreatine kinase activity
C0005524molecular_functionATP binding
C0005615cellular_componentextracellular space
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
C0046314biological_processphosphocreatine biosynthetic process
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0004054molecular_functionarginine kinase activity
D0004111molecular_functioncreatine kinase activity
D0005524molecular_functionATP binding
D0005615cellular_componentextracellular space
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
D0046314biological_processphosphocreatine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ARG A 5001
ChainResidue
AASN54
AHOH955
AHOH1662
APHE61
AHIS62
ALEU63
AGLY64
AHIS191
AGLU222
ACYS274
ASER276

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ANP A 6001
ChainResidue
ASER118
AARG120
AARG122
AHIS181
ATRP218
AARG226
AMSE230
AARG283
ASER285
AVAL286
AHIS287
AARG311
AASP326
AHOH485
AHOH569
AHOH837
AHOH1074
AHOH1112

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 Residues60
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00843","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon