Structure of PDB 3mat Chain A

Receptor sequence

>3matA (length=264) Species: 562 (Escherichia coli)

AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGQGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHDEL

3D structure

• PDB: 3mat Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis.
• Chain: A
• Resolution: 2.0 Å

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.

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	peptide	A	H63 Y65 H79 D97 D108 Y168 H171 F177 H178 E204 E235	H62 Y64 H78 D96 D107 Y167 H170 F176 H177 E203 E234
BS02	CO	A	D108 H171 E204 E235	D107 H170 E203 E234
BS03	CO	A	D97 D108 E235	D96 D107 E234

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)