Structure of PDB 2bb7 Chain A

Receptor sequence
>2bb7A (length=258) Species: 562 (Escherichia coli) [Search protein sequence]
IKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQH
AVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKDG
FHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAIQ
KFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTIE
PMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDD
TIPAIISH
3D structure
PDB2bb7 Metal mediated inhibition of methionine aminopeptidase by quinolinyl sulfonamides
ChainA
Resolution1.7 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) H75 D93 D104 H167 R171 H174 Q178 E200 N204 Q229 E231
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 D97 D108 E235 D93 D104 E231
BS02 MN A D108 H171 T202 E204 E235 D104 H167 T198 E200 E231
BS03 QMS A C59 Y62 C70 H79 F177 H178 W221 C55 Y58 C66 H75 F173 H174 W217 MOAD: ic50=2.14uM
PDBbind-CN: -logKd/Ki=5.67,IC50=2.14uM
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:2bb7, PDBe:2bb7, PDBj:2bb7
PDBsum2bb7
PubMed16300729
UniProtP0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)

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