Structure of PDB 1vrp Chain A

Receptor sequence
>1vrpA (length=370) Species: 7787 (Tetronarce californica) [Search protein sequence]
LNYSAAEEFPDLSKHNNHMAKALTLDIYKKLRDKETPSGFTLDDIIQTGV
DNPGHPFIMTVGCVAGDEECYEVFKDLFDPVIEDRHGGYKPTDKHKTDLN
QENLKGGDDLDPNYVLSSRVRTGRSIKGIALPPHCSRGERRLVEKLCIDG
LATLTGEFQGKYYPLSSMSDAEQQQLIDDHFLFDKPISPLLLASGMARDW
PDGRGIWHNNDKTFLVWVNEEDHLRVISMQKGGNMKEVFRRFCVGLKKIE
DIFVKAGRGFMWNEHLGYVLTCPSNLGTGLRGGVHVKIPHLCKHEKFSEV
LKRTRLQKRGTGGVDTAAVGSIYDISNADRLGFSEVEQVQMVVDGVKLMV
EMEKRLENGKSIDDLMPAQK
3D structure
PDB1vrp The 2.1 A Structure of Torpedo californica Creatine Kinase Complexed with the ADP-Mg(2+)-NO3(-)-Creatine Transition-State Analogue Complex
ChainA
Resolution2.1 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 V325
Catalytic site (residue number reindexed from 1) R121 E221 R225 C272 S274 R281 R309 V314
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 S128 R130 R132 H191 R292 G294 V295 H296 T322 D335 S117 R119 R121 H180 R281 G283 V284 H285 T311 D324
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004111 creatine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
Biological Process
GO:0016310 phosphorylation
GO:0046314 phosphocreatine biosynthetic process
Cellular Component
GO:0005615 extracellular space
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1vrp, PDBe:1vrp, PDBj:1vrp
PDBsum1vrp
PubMed12437342
UniProtP04414|KCRM_TETCF Creatine kinase M-type

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