6IZI

Crystal structure of E. coli peptide deformylase and methionine aminopeptidase fitted into the cryo-EM density map of the complex

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0005515	molecular_function	protein binding
P	0005829	cellular_component	cytosol
P	0006412	biological_process	translation
P	0008198	molecular_function	ferrous iron binding
P	0008270	molecular_function	zinc ion binding
P	0016787	molecular_function	hydrolase activity
P	0042586	molecular_function	peptide deformylase activity
P	0043022	molecular_function	ribosome binding
P	0043686	biological_process	co-translational protein modification
P	0046872	molecular_function	metal ion binding
Q	0004177	molecular_function	aminopeptidase activity
Q	0004239	molecular_function	initiator methionyl aminopeptidase activity
Q	0005829	cellular_component	cytosol
Q	0006508	biological_process	proteolysis
Q	0008198	molecular_function	ferrous iron binding
Q	0008235	molecular_function	metalloexopeptidase activity
Q	0046872	molecular_function	metal ion binding
Q	0046914	molecular_function	transition metal ion binding
Q	0070006	molecular_function	metalloaminopeptidase activity

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
Q	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
Q	HIS79
Q	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
Q	ASP97
Q	ASP108
Q	HIS171
Q	GLU204
Q	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
Q	THR99

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 98

Chain	Residue	Details
P	GLY45	activator, hydrogen bond acceptor
P	GLN50	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
P	CYS90	metal ligand
P	LEU91	electrostatic stabiliser, hydrogen bond donor
P	HIS132	metal ligand
P	GLU133	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
P	HIS136	metal ligand

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