Structure of PDB 2gg5 Chain A

Receptor sequence

>2gg5A (length=263) Species: 83333 (Escherichia coli K-12)

AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHDE

3D structure

• PDB: 2gg5 Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors.
• Chain: A
• Resolution: 2.12 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): H78 D96 D107 H170 R174 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	CO	A	D108 H171 T202 E204 E235	D107 H170 T201 E203 E234
BS02	CO	A	D97 D108 E235	D96 D107 E234
BS03	U19	A	Y62 Y65 D97 H171 F177 H178 E204 W221	Y61 Y64 D96 H170 F176 H177 E203 W220	MOAD: ic50=0.25uM PDBbind-CN: -logKd/Ki=6.60,IC50=0.25uM BindingDB: IC50=250nM

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:2gg5, PDBe:2gg5, PDBj:2gg5
• PDBsum: 2gg5
• PubMed: 17120228
• UniProt: P0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)