2EVC
Crystal structure of E. Coli. methionine amino peptidase in complex with 5-(2-(trifluoromethyl)phenyl)furan-2-carboxylic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0004239 | molecular_function | initiator methionyl aminopeptidase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005829 | cellular_component | cytosol |
A | 0006508 | biological_process | proteolysis |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0008233 | molecular_function | peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 901 |
Chain | Residue |
A | ASP97 |
A | ASP108 |
A | GLU235 |
A | MN902 |
A | FC3999 |
A | HOH1010 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 902 |
Chain | Residue |
A | GLU235 |
A | MN901 |
A | FC3999 |
A | ASP108 |
A | HIS171 |
A | GLU204 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 903 |
Chain | Residue |
A | ASN74 |
A | VAL76 |
A | SER231 |
A | HOH1009 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE FC3 A 999 |
Chain | Residue |
A | CYS59 |
A | TYR62 |
A | HIS63 |
A | TYR65 |
A | CYS70 |
A | HIS79 |
A | ASP97 |
A | ASP108 |
A | HIS171 |
A | PHE177 |
A | HIS178 |
A | GLU204 |
A | TRP221 |
A | GLU235 |
A | MN901 |
A | MN902 |
Functional Information from PROSITE/UniProt
site_id | PS00680 |
Number of Residues | 19 |
Details | MAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGrgfHeepqVl.HY |
Chain | Residue | Details |
A | TYR168-TYR186 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01974","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10387007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18093325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18785729","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10555963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17120228","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a16 |
Chain | Residue | Details |
A | GLU204 | |
A | GLN182 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1a16 |
Chain | Residue | Details |
A | GLU204 |