Structure of PDB 2crk Chain A

Receptor sequence
>2crkA (length=365) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
NKYKLNYKSEEEYPDLSKHNNHMAKVLTPDLYKKLRDKETPSGFTLDDVI
QTGVDNPGHPFIMTVGCVAGDEESYTVFKDLFDPIIQDRHGGFKPTDKHK
TDLNHENLKGGDDLDPHYVLSSRVRTGRSIKGYTLPPHCSRGERRAVEKL
SVEALNSLTGEFKGKYYPLKSMTEQEQQQLIDDHFLFDKPVSPLLLASGM
ARDWPDARGIWHNDNKSFLVWVNEEDHLRVISMEKGGNMKEVFRRFCVGL
QKIEEIFKKAGHPFMWNEHLGYVLTCPSNLGTGLRGGVHVKLAHLSKHPK
FEEILTRLRLQKRGTSVFDISNADRLGSSEVEQVQLVVDGVKLMVEMEKK
LEKGQSIDDMIPAQK
3D structure
PDB2crk Crystal structure of rabbit muscle creatine kinase.
ChainA
Resolution2.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R132 E232 R236 C283 S285 R292 R320
Catalytic site (residue number reindexed from 1) R125 E225 R229 C276 S278 R285 R313
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 SO4 A R132 R320 R125 R313
BS02 SO4 A R130 R132 R123 R125
BS03 SO4 A R96 S285 R89 S278
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:2crk, PDBe:2crk, PDBj:2crk
PDBsum2crk
PubMed9849893
UniProtP00563|KCRM_RABIT Creatine kinase M-type (Gene Name=CKM)

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