Structure of PDB 2bmu Chain B

Receptor sequence

>2bmuB (length=226) Species: 2261 (Pyrococcus furiosus)

AMRIVFDIGGSVLVPENPDIDFIKEIAYQLTKVSEDHEVAVVVGGGKLAR
KYIEVAEKFNSSETFKDFIGIQITRANAMLLIAALREKAYPVVVEDFWEA
WKAVQLKKIPVMGGTHPGHTTDAVAALLAEFLKADLLVVITNVDGVYTAD
PKKDPTAKKIKKMKPEELLEIVGKGIEKAGSSSVIDPLAAKIIARSGIKT
IVIGKEDAKDLFRVIKGDHNGTTIEP

3D structure

• PDB: 2bmu The Crystal Structure of Pyrococcus Furiosus Ump Kinase Provides Insight Into Catalysis and Regulation in Microbial Pyrimidine Nucleotide Biosynthesis.
• Chain: B
• Resolution: 2.55 Å

Enzymatic activity

• Enzyme Commision number: 2.7.4.22: UMP 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	MG	B	D6 D121	D7 D122
BS02	ANP	B	G8 G9 G43 G44 G45 T140 N141 V145 Y146 A148 D149 P150 S181 S182 V183	G9 G10 G44 G45 G46 T141 N142 V146 Y147 A149 D150 P151 S182 S183 V184
BS03	U5P	B	G43 G44 D66 G69 I70 G113 T114 H115 H118 T119 T120 A178	G44 G45 D67 G70 I71 G114 T115 H116 H119 T120 T121 A179
BS04	MG	B	D121 S182 V183	D122 S183 V184

Gene Ontology

Molecular Function

• GO:0005524 ATP binding
• GO:0009041 UMP/dUMP kinase activity
• GO:0016301 kinase activity
• GO:0033862 UMP kinase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006221 pyrimidine nucleotide biosynthetic process
• GO:0006225 UDP biosynthetic process
• GO:0016310 phosphorylation
• GO:0044210 'de novo' CTP biosynthetic process
• GO:0046940 nucleoside monophosphate phosphorylation

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2bmu, PDBe:2bmu, PDBj:2bmu
• PDBsum: 2bmu
• PubMed: 16095620
• UniProt: Q8U122|PYRH_PYRFU Uridylate kinase (Gene Name=pyrH)