6J0A
Crystal structure of E. coli methionine aminopeptidase enzyme and chaperone trigger factor fitted into the cryo-EM density map of the complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
P | 0004177 | molecular_function | aminopeptidase activity |
P | 0004239 | molecular_function | initiator methionyl aminopeptidase activity |
P | 0005829 | cellular_component | cytosol |
P | 0006508 | biological_process | proteolysis |
P | 0008198 | molecular_function | ferrous iron binding |
P | 0008235 | molecular_function | metalloexopeptidase activity |
P | 0046872 | molecular_function | metal ion binding |
P | 0046914 | molecular_function | transition metal ion binding |
P | 0070006 | molecular_function | metalloaminopeptidase activity |
Q | 0003677 | molecular_function | DNA binding |
Q | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
Q | 0005515 | molecular_function | protein binding |
Q | 0005737 | cellular_component | cytoplasm |
Q | 0006457 | biological_process | protein folding |
Q | 0015031 | biological_process | protein transport |
Q | 0032784 | biological_process | regulation of DNA-templated transcription elongation |
Q | 0043022 | molecular_function | ribosome binding |
Q | 0043335 | biological_process | protein unfolding |
Q | 0044183 | molecular_function | protein folding chaperone |
Q | 0051083 | biological_process | 'de novo' cotranslational protein folding |
Q | 0051301 | biological_process | cell division |
Q | 0061077 | biological_process | chaperone-mediated protein folding |
Functional Information from PROSITE/UniProt
site_id | PS00680 |
Number of Residues | 19 |
Details | MAP_1 Methionine aminopeptidase subfamily 1 signature. YcGHGIGqgfHeepqVl.HY |
Chain | Residue | Details |
P | TYR168-TYR186 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228 |
Chain | Residue | Details |
P | HIS79 | |
P | HIS178 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729 |
Chain | Residue | Details |
P | ASP97 | |
P | ASP108 | |
P | HIS171 | |
P | GLU204 | |
P | GLU235 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228 |
Chain | Residue | Details |
P | THR99 |