Structure of PDB 1cli Chain C

Receptor sequence
>1cliC (length=341) Species: 562 (Escherichia coli) [Search protein sequence]
TSLSYKDAGVDIDAGNALVGRIKGVVKKTRRPEVMGGLGGFGALCALPQK
YREPVLVSGTDGVGTKLRLAMDLKRHDTIGIDLVAMCVNDLVVQGAEPLF
FLDYYATGKLDVDTASAVISGIAEGCLQSGCSLVGGETAEMPGMYHGEDY
DVAGFCVGVVEKSEIIDGSKVSDGDVLIALGSSGPHSNGYSLVRKILEVS
GCDPQTTELDGKPLADHLLAPTRIYVKSVLELIEKVDVHAIAHLTGGGFW
ENIPRVLPDNTQAVIDESSWQWPEVFNWLQTAGNVEHHEMYRTFNCGVGM
IIALPAPEVDKALALLNANGENAWKIGIIKASDSEQRVVIE
3D structure
PDB1cli X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution.
ChainC
Resolution2.5 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 6.3.3.1: phosphoribosylformylglycinamidine cyclo-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 SO4 C T2069 N2192 G2193 Y2194 S2195 T65 N188 G189 Y190 S191
Gene Ontology
Molecular Function
GO:0004637 phosphoribosylamine-glycine ligase activity
GO:0004641 phosphoribosylformylglycinamidine cyclo-ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0046084 adenine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1cli, PDBe:1cli, PDBj:1cli
PDBsum1cli
PubMed10508786
UniProtP08178|PUR5_ECOLI Phosphoribosylformylglycinamidine cyclo-ligase (Gene Name=purM)

[Back to BioLiP]