Structure of PDB 1gyt Chain I Binding Site BS01

Receptor Information
>1gyt Chain I (length=503) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRG
ELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTL
NDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEP
RRPLRKMVFNVPTRRELTSGERAIQHGLAIAAGIKAAKDLGNMPPNICNA
AYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMS
VIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAV
YGVMRMVAELQLPINVIGVLAGCENMPGGRAYRPGDVLTTMSGQTVEVLN
TDAEGRLVLCDVLTYVERFEPEAVIDVATLTGACVIALGHHITGLMANHN
PLAHELIAASEQSGDRAWRLPLGDEYQEQLESNFADMANIGGRPGGAITA
GCFLSRFTRKYNWAHLDIAGTAWRSGKAKGATGRPVALLAQFLLNRAGFN
GEE
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1gyt Chain I Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1gyt X-Ray Structure of Aminopeptidase a from Escherichia Coli and a Model for the Nucleoprotein Complex in Xer Site-Specific Recombination
Resolution2.5 Å
Binding residue
(original residue number in PDB)		K270 D275 D293 E354
Binding residue
(residue number reindexed from 1)		K270 D275 D293 E354
Annotation score4
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.
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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Biological Process
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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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