Structure of PDB 3x2s Chain A

Receptor sequence
>3x2sA (length=214) Species: 1110693 (Escherichia coli str. K-12 substr. MDS42) [Search protein sequence]
MRIILLGAPGAGKGTQAQFIMEKYGIPQISTGDMLRAAVKSGSELGKQAK
DIMDCGKLVTDELVIALVKERIAQEDSRNGFLLDGFPRTIPQADAMKEAG
INVDYVLEFDVPDELIVDRIVGRRVHAPSGRVYHVKFNPPKVEGKDDVTG
EELTTRKDDQEETVRKRLCEYHQMTAPLIGYYSKEAEAGNTKYAKVDGTK
PVAEVRADLEKILG
3D structure
PDB3x2s Excimer Emission Properties on Pyrene-Labeled Protein Surface: Correlation between Emission Spectra, Ring Stacking Modes, and Flexibilities of Pyrene Probes.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K13 R88 R123 R156 R167
Catalytic site (residue number reindexed from 1) K13 R88 R123 R156 R167
Enzyme Commision number 2.7.4.3: adenylate kinase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004017 adenylate kinase activity
GO:0004550 nucleoside diphosphate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016776 phosphotransferase activity, phosphate group as acceptor
GO:0019205 nucleobase-containing compound kinase activity
GO:0050145 nucleoside monophosphate kinase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0009123 nucleoside monophosphate metabolic process
GO:0009132 nucleoside diphosphate metabolic process
GO:0009165 nucleotide biosynthetic process
GO:0016310 phosphorylation
GO:0044209 AMP salvage
GO:0046940 nucleoside monophosphate phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3x2s, PDBe:3x2s, PDBj:3x2s
PDBsum3x2s
PubMed25646669
UniProtA0A0J9X1X4

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