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

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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

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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

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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

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