Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0004239 | molecular_function | initiator methionyl aminopeptidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008235 | molecular_function | metalloexopeptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070006 | molecular_function | metalloaminopeptidase activity |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0004239 | molecular_function | initiator methionyl aminopeptidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008235 | molecular_function | metalloexopeptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 501 |
| Chain | Residue |
| B | ASP82 |
| B | ASP93 |
| B | GLU280 |
| B | CO502 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 502 |
| Chain | Residue |
| B | ASP93 |
| B | HIS153 |
| B | GLU187 |
| B | GLU280 |
| B | CO501 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO B 503 |
| Chain | Residue |
| A | HIS173 |
| B | HIS62 |
| B | HOH604 |
| B | HOH651 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO A 504 |
| Chain | Residue |
| A | ASP82 |
| A | ASP93 |
| A | GLU280 |
| A | CO505 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 505 |
| Chain | Residue |
| A | ASP93 |
| A | HIS153 |
| A | GLU187 |
| A | GLU280 |
| A | CO504 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CO A 506 |
| Chain | Residue |
| A | HIS62 |
| B | HIS173 |
Functional Information from PROSITE/UniProt
| site_id | PS01202 |
| Number of Residues | 17 |
| Details | MAP_2 Methionine aminopeptidase subfamily 2 signature. DYlKIDvGvHIDGfiaD |
| Chain | Residue | Details |
| A | ASP77-ASP93 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01975","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU187 | |
| A | SER165 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| B | GLU187 | |
| B | SER165 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU187 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| B | GLU187 | |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 917 |
| Chain | Residue | Details |
| A | ASP82 | metal ligand |
| A | ASP93 | metal ligand |
| A | HIS153 | metal ligand |
| A | HIS161 | electrostatic stabiliser |
| A | GLU187 | metal ligand, proton acceptor, proton donor |
| A | GLU280 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 917 |
| Chain | Residue | Details |
| B | ASP82 | metal ligand |
| B | ASP93 | metal ligand |
| B | HIS153 | metal ligand |
| B | HIS161 | electrostatic stabiliser |
| B | GLU187 | metal ligand, proton acceptor, proton donor |
| B | GLU280 | metal ligand |
