Structure of PDB 1u6r Chain A

Receptor sequence
>1u6rA (length=380) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
PFGNTHNKYKLNYKSEEEYPDLSKHNNHMAKVLTPDLYKKLRDKETPSGF
TLDDVIQTGVDNPGHPFIMTVGCVAGDEESYTVFKDLFDPIIQDRHGGFK
PTDKHKTDLNHENLKGGDDLDPHYVLSSRVRTGKSIKGYTLPPHCSRGER
RAVEKLSVEALNSLTGEFKGKYYPLKSMTEQEQQQLIDDHFLFDKPVSPL
LLASGMARDWPDARGIWHNDNKSFLVWVNEEDHLRVISMEKGGNMKEVFR
RFCVGLQKIEEIFKKAGHPFMWNEHLGYVLTCPSNLGTGLRGGVHVKLAH
LSKHPKFEEILTRLRLQKRGTGGVDTAAVGSVFDISNADRLGSSEVEQVQ
LVVDGVKLMVEMEKKLEKGQSIDDMIPAQK
3D structure
PDB1u6r Structural asymmetry and intersubunit communication in muscle creatine kinase
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R131 E231 R235 C282 S284 R291 R319 V324
Catalytic site (residue number reindexed from 1) R131 E231 R235 C282 S284 R291 R319 V324
Enzyme Commision number 2.7.3.2: creatine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP A S127 R129 R131 R235 R291 V294 H295 R319 G322 G323 D334 S127 R129 R131 R235 R291 V294 H295 R319 G322 G323 D334
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004111 creatine kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
Biological Process
GO:0009408 response to heat
GO:0016310 phosphorylation
GO:0046314 phosphocreatine biosynthetic process
Cellular Component
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1u6r, PDBe:1u6r, PDBj:1u6r
PDBsum1u6r
PubMed17327675
UniProtP00563|KCRM_RABIT Creatine kinase M-type (Gene Name=CKM)

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