Structure of PDB 1gyt Chain D

Receptor sequence
>1gytD (length=503) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRG
ELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTL
NDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEP
RRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNA
AYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMS
VIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAV
YGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLN
TDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHN
PLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITA
GCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFN
GEE
3D structure
PDB1gyt X-Ray Structure of Aminopeptidase a from Escherichia Coli and a Model for the Nucleoprotein Complex in Xer Site-Specific Recombination
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) K282 R356
Catalytic site (residue number reindexed from 1) K282 R356
Enzyme Commision number 3.4.11.1: leucyl aminopeptidase.
3.4.11.10: bacterial leucyl aminopeptidase.
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 D K270 D275 D293 E354 K270 D275 D293 E354
BS02 ZN D D275 D352 E354 D275 D352 E354
BS03 CO3 D A353 G355 R356 L380 A353 G355 R356 L380
Gene Ontology
Molecular Function
GO:0001073 transcription antitermination factor activity, DNA binding
GO:0003677 DNA binding
GO:0004177 aminopeptidase activity
GO:0008235 metalloexopeptidase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006276 plasmid maintenance
GO:0006351 DNA-templated transcription
GO:0006508 proteolysis
GO:0019538 protein metabolic process
GO:0031564 transcription antitermination
GO:0042150 plasmid recombination
GO:0043171 peptide catabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1gyt, PDBe:1gyt, PDBj:1gyt
PDBsum1gyt
PubMed10449417
UniProtP68767|AMPA_ECOLI Cytosol aminopeptidase (Gene Name=pepA)

[Back to BioLiP]