Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3DRE

Crystal structure of Human Brain-type Creatine Kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004111molecular_functioncreatine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0016301molecular_functionkinase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0021762biological_processsubstantia nigra development
A0031625molecular_functionubiquitin protein ligase binding
A0046314biological_processphosphocreatine biosynthetic process
A0070062cellular_componentextracellular exosome
A0140651biological_processfutile creatine cycle
B0003824molecular_functioncatalytic activity
B0004111molecular_functioncreatine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0016301molecular_functionkinase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0021762biological_processsubstantia nigra development
B0031625molecular_functionubiquitin protein ligase binding
B0046314biological_processphosphocreatine biosynthetic process
B0070062cellular_componentextracellular exosome
B0140651biological_processfutile creatine cycle
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 Residues22
DetailsBINDING: BINDING => ECO:0000269|PubMed:18977227
ChainResidueDetails
AVAL72
AARG320
AASP335
BVAL72
BSER128
BARG130
BARG132
BHIS191
BGLU232
BARG236
BSER285
ASER128
BARG292
BARG320
BASP335
AARG130
AARG132
AHIS191
AGLU232
AARG236
ASER285
AARG292

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER4
BSER4

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR35
BTHR35

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q04447
ChainResidueDetails
ATYR125
BTYR125

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER199
BSER199

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q04447
ChainResidueDetails
ATYR269
BTYR269

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07335
ChainResidueDetails
ASER309
BSER309

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q04447
ChainResidueDetails
ATHR322
BTHR322

site_idSWS_FT_FI9
Number of Residues10
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33268465
ChainResidueDetails
ALYS45
BLYS381
ALYS101
ALYS107
ALYS381
BLYS45
BLYS101
BLYS107

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

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon