6S07

Structure of formylglycine-generating enzyme at 1.04 A in complex with copper and substrate reveals an acidic pocket for binding and acti-vation of molecular oxygen.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016491	molecular_function	oxidoreductase activity
A	0018158	biological_process	protein oxidation
A	0043687	biological_process	post-translational protein modification
A	0046872	molecular_function	metal ion binding
A	0120147	molecular_function	formylglycine-generating oxidase activity
A	1903136	molecular_function	cuprous ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue CU1 A 401

Chain	Residue
A	CYS269
A	CYS274
C	CYS7

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site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 402

Chain	Residue
A	ASN222
A	VAL223
A	GLY225
A	VAL227
A	GLU229
A	GLY265

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site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 403

Chain	Residue
A	ASN188
A	ILE189
A	ASP202
A	TYR204
A	HOH532
A	HOH539

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site_id	AC4
Number of Residues	3
Details	binding site for residue CL A 404

Chain	Residue
A	PRO131
A	ASN132
A	HIS133

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28544744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NYY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27862795","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28544744","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5NXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5NYY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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