Structure of PDB 3mat Chain A Binding Site BS01

Receptor Information

>3mat Chain A (length=264) Species: 562 (Escherichia coli)

AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGQGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHDEL

Ligand information

>3mat Chain I (length=3)

KAL

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3mat Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): H63 Y65 H79 D97 D108 Y168 H171 F177 H178 E204 E235
• Binding residue (residue number reindexed from 1): H62 Y64 H78 D96 D107 Y167 H170 F176 H177 E203 E234

Enzymatic activity

• Catalytic site (original residue number in PDB): H79 D97 D108 H171 Q175 H178 Q182 E204 N208 Q233 E235
• Catalytic site (residue number reindexed from 1): H78 D96 D107 H170 Q174 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:3mat, PDBe:3mat, PDBj:3mat
• PDBsum: 3mat
• PubMed: 10387007
• UniProt: P0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)