Structure of PDB 1u9z Chain D

Receptor sequence
>1u9zD (length=274) Species: 2190 (Methanocaldococcus jannaschii) [Search protein sequence]
MIVVSGSQSQNLAFKVAKLLNTKLTRVEYKRFPDNEIYVRIVDEINDDEA
VIINTQKNQNDAIVETILLCDALRDEGVKKITLVAPYLAYARQDKKFNPG
EAISIRALAKIYSNIVDKLITINPHETHIKDFFTIPFIYGDAVPKLAEYV
KDKLNDPIVLAPDKGALEFAKTASKILNAEYDYLEIAPKTLDAKDRDVFI
VDDIISTGGTMATAVKLLKEQGAKKIIAACVHPVLIGDALNKLYSAGVEE
VVGTDTYLSEVSKVSVAEVIVDLL
3D structure
PDB1u9z Novel class III phosphoribosyl diphosphate synthase: structure and properties of the tetrameric, phosphate-activated, non-allosterically inhibited enzyme from Methanocaldococcus jannaschii
ChainD
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.6.1: ribose-phosphate diphosphokinase.
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 AMP D R92 Q93 F97 H125 R92 Q93 F97 H125
BS02 R5P D D163 D212 I215 S216 T217 G218 T220 D163 D202 I205 S206 T207 G208 T210
BS03 AMP D F32 D34 E36 F32 D34 E36
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004749 ribose phosphate diphosphokinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0006015 5-phosphoribose 1-diphosphate biosynthetic process
GO:0006164 purine nucleotide biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0016310 phosphorylation
Cellular Component
GO:0002189 ribose phosphate diphosphokinase complex
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:1u9z, PDBe:1u9z, PDBj:1u9z
PDBsum1u9z
PubMed16288921
UniProtQ58761|KPRS_METJA Ribose-phosphate pyrophosphokinase (Gene Name=prs)

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