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1I0E

CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004111molecular_functioncreatine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0016301molecular_functionkinase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046314biological_processphosphocreatine biosynthetic process
B0003824molecular_functioncatalytic activity
B0004111molecular_functioncreatine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0016301molecular_functionkinase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0046314biological_processphosphocreatine biosynthetic process
C0003824molecular_functioncatalytic activity
C0004111molecular_functioncreatine kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0016301molecular_functionkinase activity
C0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
C0046314biological_processphosphocreatine biosynthetic process
D0003824molecular_functioncatalytic activity
D0004111molecular_functioncreatine kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0016301molecular_functionkinase activity
D0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
D0046314biological_processphosphocreatine biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00112
Number of Residues7
DetailsPHOSPHAGEN_KINASE Phosphagen kinase active site signature. CP.SNLGT
ChainResidueDetails
ACYS283-THR289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843
ChainResidueDetails
ASER128
BARG292
BARG320
BASP335
CSER128
CHIS191
CARG236
CARG292
CARG320
CASP335
DSER128
AHIS191
DHIS191
DARG236
DARG292
DARG320
DASP335
AARG236
AARG292
AARG320
AASP335
BSER128
BHIS191
BARG236

site_idSWS_FT_FI2
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07310
ChainResidueDetails
ASER164
DSER164
DSER199
DSER372
ASER199
ASER372
BSER164
BSER199
BSER372
CSER164
CSER199
CSER372

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00564
ChainResidueDetails
ATHR166
DTHR166
DTHR180
DTHR313
ATHR180
ATHR313
BTHR166
BTHR180
BTHR313
CTHR166
CTHR180
CTHR313

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00564
ChainResidueDetails
ASER178
BSER178
CSER178
DSER178

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07310
ChainResidueDetails
ATHR322
BTHR322
CTHR322
DTHR322

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
AARG236
AARG292
AARG320
AARG132
AGLU232

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
BARG236
BARG292
BARG320
BARG132
BGLU232

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
CARG236
CARG292
CARG320
CARG132
CGLU232

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bg0
ChainResidueDetails
DARG236
DARG292
DARG320
DARG132
DGLU232

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PDB entries from 2024-05-01

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