Structure of PDB 3d27 Chain A

Receptor sequence
>3d27A (length=261) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQ
HAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKD
GFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAI
QKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTI
EPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKD
DTIPAIISHDE
3D structure
PDB3d27 Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II)-form selectivity and antibacterial activity.
ChainA
Resolution2.2 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 R175 H178 Q182 E204 N208 Q233 E235
Catalytic site (residue number reindexed from 1) H76 D94 D105 H168 R172 H175 Q179 E201 N205 Q230 E232
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 MN A D108 H171 E204 E235 D105 H168 E201 E232
BS02 MN A D97 D108 E235 D94 D105 E232
BS03 W29 A Y62 Y65 H79 D97 D108 H171 H178 E204 Y59 Y62 H76 D94 D105 H168 H175 E201 MOAD: ic50=55.7uM
PDBbind-CN: -logKd/Ki=4.25,IC50=55.7uM
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004239 initiator methionyl aminopeptidase activity
GO:0008198 ferrous iron binding
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:3d27, PDBe:3d27, PDBj:3d27
PDBsum3d27
PubMed18785729
UniProtP0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)

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