Structure of PDB 1rae Chain B

Receptor sequence
>1raeB (length=153) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLNLPS
GEMGRKDLIKIENTFLSEDQVDQLALYAPQATVNRIDNYEVVGKSRPSLP
ERIDNVLVCPNSNCISHAEPVSSSFAVRKRANDIALKCKYCEKEFSHNVV
LAN
3D structure
PDB1rae Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity.
ChainB
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 ?
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 ZN B C109 C114 C138 C141 C109 C114 C138 C141
BS02 CTP B A11 I12 K60 N84 Y89 V91 K94 A11 I12 K60 N84 Y89 V91 K94
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0009347 aspartate carbamoyltransferase complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1rae, PDBe:1rae, PDBj:1rae
PDBsum1rae
PubMed8441751
UniProtP0A7F3|PYRI_ECOLI Aspartate carbamoyltransferase regulatory chain (Gene Name=pyrI)

[Back to BioLiP]