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1QH4

CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004111molecular_functioncreatine kinase activity
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006754biological_processATP biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0046314biological_processphosphocreatine biosynthetic process
A0065010cellular_componentextracellular membrane-bounded organelle
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004111molecular_functioncreatine kinase activity
B0005524molecular_functionATP binding
B0005615cellular_componentextracellular space
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006754biological_processATP biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0046314biological_processphosphocreatine biosynthetic process
B0065010cellular_componentextracellular membrane-bounded organelle
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004111molecular_functioncreatine kinase activity
C0005524molecular_functionATP binding
C0005615cellular_componentextracellular space
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006754biological_processATP biosynthetic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
C0046314biological_processphosphocreatine biosynthetic process
C0065010cellular_componentextracellular membrane-bounded organelle
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0004111molecular_functioncreatine kinase activity
D0005524molecular_functionATP binding
D0005615cellular_componentextracellular space
D0005739cellular_componentmitochondrion
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006754biological_processATP biosynthetic process
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
D0046314biological_processphosphocreatine biosynthetic process
D0065010cellular_componentextracellular membrane-bounded organelle
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA D 382
ChainResidue
DLYS41
DASP44

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 1501
ChainResidue
BSER15
BVAL16
BARG43
BHOH1850

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 1502
ChainResidue
AHOH1662
AHOH1692
AHOH1834
ATHR71
AVAL72
ALEU201

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 1503
ChainResidue
BTHR71
BVAL72
BLEU201
BHOH1574
BHOH1706
BHOH1833

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT C 1504
ChainResidue
CTHR71
CVAL72
CLEU201
CHOH1638
CHOH1728
CHOH1788

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT C 1505
ChainResidue
CASN222
CTHR224
CGLN241
CLYS242
CHOH1653

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT D 1506
ChainResidue
DTHR71
DVAL72
DLEU201
DHOH1552
DHOH1604
DHOH1616

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 Residues348
DetailsDomain: {"description":"Phosphagen kinase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00842","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues968
DetailsDomain: {"description":"Phosphagen kinase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00843","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P12277","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues64
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00843","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"7669815","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"7669815","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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 2025-12-17

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