Structure of PDB 2bne Chain B

Receptor sequence
>2bneB (length=238) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TNAKPVYKRILLKLSGEALQGTEFGIDASILDRMAQEIKELVELGIQVGV
VIGGGNLFRGAGLAKAGMNRVVGDHMGMLATVMNGLAMRDALHRAYVNAR
LMSAIPLNGVCDSYSWAEAISLLRNNRVVILSAGTGNPFFTTDSAACLRG
IEIEANVVLKATKVDGVFTADPAKDPTATMYEQLTYSEVLEKELKVMDLA
AFTLARDHKLPIRVFNMNKPGALRRVVMGEKEGTLITE
3D structure
PDB2bne Structure of Escherichia Coli Ump Kinase Differs from that of Other Nucleoside Monophosphate Kinases and Sheds New Light on Enzyme Regulation.
ChainB
Resolution2.3 Å
3D
structure
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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 U5P B G56 G57 G58 R62 G63 D77 G80 M81 T138 N140 F143 T144 T145 G53 G54 G55 R59 G60 D74 G77 M78 T135 N137 F140 T141 T142
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0009041 UMP/dUMP kinase activity
GO:0016301 kinase activity
GO:0033862 UMP kinase activity
GO:0042802 identical protein 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
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2bne, PDBe:2bne, PDBj:2bne
PDBsum2bne
PubMed15857829
UniProtP0A7E9|PYRH_ECOLI Uridylate kinase (Gene Name=pyrH)

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