Structure of PDB 1gyt Chain I

Receptor sequence
>1gytI (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
ChainI
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 I K270 D275 D293 E354 K270 D275 D293 E354
BS02 ZN I D275 D352 E354 D275 D352 E354
BS03 CO3 I A353 E354 G355 R356 L380 A353 E354 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

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

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