Structure of PDB 2q92 Chain A Binding Site BS01

Receptor Information

>2q92 Chain A (length=262) Species: 562 (Escherichia coli)

AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHD

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 2q92 Chain A Residue 300

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2q92 Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop flexibility in selective inhibition of bacterial enzymes.
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): D108 H171 E204 E235
• Binding residue (residue number reindexed from 1): D107 H170 E203 E234
• Annotation score: 4

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.

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:2q92, PDBe:2q92, PDBj:2q92
• PDBsum: 2q92
• PubMed: 18093325
• UniProt: P0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)