Structure of PDB 4pnc Chain A

Receptor sequence
>4pncA (length=262) Species: 562 (Escherichia coli) [Search protein sequence]
AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGQGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHD
3D structure
PDB4pnc Beta-aminoketones as prodrugs for selective irreversible inhibitors of type-1 methionine aminopeptidases.
ChainA
Resolution1.54 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H79 D97 D108 H171 Q175 H178 Q182 E204 N208 Q233 E235
Catalytic site (residue number reindexed from 1) H78 D96 D107 H170 Q174 H177 Q181 E203 N207 Q232 E234
Enzyme Commision number 3.4.11.18: methionyl 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 7NP A C59 Y65 C70 H79 F177 H178 C58 Y64 C69 H78 F176 H177 PDBbind-CN: -logKd/Ki=5.43,IC50=3.7uM
BS02 CO A D97 D108 E235 D96 D107 E234
BS03 CO A D108 H171 T202 E204 E235 D107 H170 T201 E203 E234
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004239 initiator methionyl aminopeptidase activity
GO:0008235 metalloexopeptidase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4pnc, PDBe:4pnc, PDBj:4pnc
PDBsum4pnc
PubMed25293447
UniProtC3TPN7

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