Structure of PDB 2r87 Chain E

Receptor sequence
>2r87E (length=334) Species: 2261 (Pyrococcus furiosus) [Search protein sequence]
MKVRIATYASHSALQILKGAKDEGFETIAFGSSKVKPLYTKYFPVADYFI
EEKYPEEELLNLNAVVVPTGSFVAHLGIELVENMKVPYFGNKRVLRWESD
RNLERKWLKKAGIRVPEVYEDPDDIEKPVIVKPHGAKGGKGYFLAKDPED
FWRKAEKFLGIKRKEDLKNIQIQEYVLGVPVYPHYFYSKVREELELMSID
RRYESNVDAIGRIPAKDQLEFDMDITYTVIGNIPIVLRESLLMDVIEAGE
RVVKAAEELMGGLWGPFCLEGVFTPDLEFVVFEISARIVAGTNIFVNGSP
YTWLRYDRPVSTGRRIAMEIREAIENDMLEKVLT
3D structure
PDB2r87 Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii.
ChainE
Resolution2.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 6.3.4.23: formate--phosphoribosylaminoimidazolecarboxamide ligase.
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 ADP E I130 K132 A136 G139 Y142 Q173 Y175 V176 E204 Y227 F282 E283 I130 K132 A136 G139 Y142 Q173 Y175 V176 E204 Y227 F282 E283
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016879 ligase activity, forming carbon-nitrogen bonds
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006188 IMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2r87, PDBe:2r87, PDBj:2r87
PDBsum2r87
PubMed18069798
UniProtQ8U0R7|PURP_PYRFU 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase (Gene Name=purP)

[Back to BioLiP]