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	0005506	molecular_function	iron ion binding
P	0005829	cellular_component	cytosol
P	0006508	biological_process	proteolysis
P	0008198	molecular_function	ferrous iron binding
P	0008233	molecular_function	peptidase activity
P	0016787	molecular_function	hydrolase activity
P	0046872	molecular_function	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	0016853	molecular_function	isomerase activity
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

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

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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

---

site_id	SWS_FT_FI4
Number of Residues	73
Details	Domain: {"description":"PPIase FKBP-type"}

Chain

Residue

Details

---