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1G0W

CRYSTAL STRUCTURE OF BOVINE RETINAL CREATINE KINASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004111molecular_functioncreatine kinase activity
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0009408biological_processresponse to heat
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046314biological_processphosphocreatine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 382
ChainResidue
AARG130
AARG132
AARG292

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 383
ChainResidue
AARG132
AASN286
AARG320
AARG341

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 Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00843
ChainResidueDetails
ASER128
AHIS191
AARG236
AARG292
AARG320
AASP335

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07310
ChainResidueDetails
ASER164
ASER199
AALA372

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P00564
ChainResidueDetails
AASP166
ATHR180
ALYS313

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00564
ChainResidueDetails
ASER178

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07310
ChainResidueDetails
ATHR322

218853

PDB entries from 2024-04-24

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