Structure of PDB 2gg0 Chain A

Receptor sequence

>2gg0A (length=262) Species: 83333 (Escherichia coli K-12)

ISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNE
QHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIK
DGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAA
IQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFT
IEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRK
DDTIPAIISHDE

3D structure

• PDB: 2gg0 Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors.
• Chain: A
• Resolution: 1.28 Å

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): H77 D95 D106 H169 R173 H176 Q180 E202 N206 Q231 E233
• 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	CO	A	D108 H171 T202 E204 E235	D106 H169 T200 E202 E233
BS02	CO	A	D97 D108 E235	D95 D106 E233
BS03	U11	A	Y62 H79 D97 D108 Y168 H171 F177 H178 E204 E235	Y60 H77 D95 D106 Y166 H169 F175 H176 E202 E233	MOAD: ic50=1.7uM PDBbind-CN: -logKd/Ki=5.77,IC50=1.7uM BindingDB: IC50=1700nM

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

External links

• PDB: RCSB:2gg0, PDBe:2gg0, PDBj:2gg0
• PDBsum: 2gg0
• PubMed: 17120228
• UniProt: P0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)