Structure of PDB 1vrp Chain B

Receptor sequence

>1vrpB (length=374) Species: 7787 (Tetronarce californica)

NKWKLNYSAAEEFPDLSKHNNHMAKALTLDIYKKLRDKETPSGFTLDDII
QTGVDNPGHPFIMTVGCVAGDEECYEVFKDLFDPVIEDRHGGYKPTDKHK
TDLNQENLKGGDDLDPNYVLSSRVRTGRSIKGIALPPHCSRGERRLVEKL
CIDGLATLTGEFQGKYYPLSSMSDAEQQQLIDDHFLFDKPISPLLLASGM
ARDWPDGRGIWHNNDKTFLVWVNEEDHLRVISMQKGGNMKEVFRRFCVGL
KKIEDIFVKAGRGFMWNEHLGYVLTCPSNLGTGLRGGVHVKIPHLCKHEK
FSEVLKRTRLQKRGTGGVDTAAVGSIYDISNADRLGFSEVEQVQMVVDGV
KLMVEMEKRLENGKSIDDLMPAQK

3D structure

• PDB: 1vrp The 2.1 A Structure of Torpedo californica Creatine Kinase Complexed with the ADP-Mg(2+)-NO3(-)-Creatine Transition-State Analogue Complex
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R132 E232 R236 C283 S285 R292 R320 V325
• Catalytic site (residue number reindexed from 1): R125 E225 R229 C276 S278 R285 R313 V318
• 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	NO3	B	R236 R320	R229 R313
BS02	ADP	B	S128 R130 R132 H191 R292 V295 H296 R320 G323 G324 V325 D335	S121 R123 R125 H184 R285 V288 H289 R313 G316 G317 V318 D328
BS03	IOM	B	T71 V72 L201 E232 C283	T64 V65 L194 E225 C276

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

External links

• PDB: RCSB:1vrp, PDBe:1vrp, PDBj:1vrp
• PDBsum: 1vrp
• PubMed: 12437342
• UniProt: P04414|KCRM_TETCF Creatine kinase M-type