Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6MUJ

Formylglycine generating enzyme bound to copper

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
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	1903135	molecular_function	cupric ion binding
B	0005509	molecular_function	calcium ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0018158	biological_process	protein oxidation
B	0043687	biological_process	post-translational protein modification
B	0046872	molecular_function	metal ion binding
B	0120147	molecular_function	formylglycine-generating oxidase activity
B	1903135	molecular_function	cupric ion binding
C	0005509	molecular_function	calcium ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0018158	biological_process	protein oxidation
C	0043687	biological_process	post-translational protein modification
C	0046872	molecular_function	metal ion binding
C	0120147	molecular_function	formylglycine-generating oxidase activity
C	1903135	molecular_function	cupric ion binding
D	0005509	molecular_function	calcium ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0018158	biological_process	protein oxidation
D	0043687	biological_process	post-translational protein modification
D	0046872	molecular_function	metal ion binding
D	0120147	molecular_function	formylglycine-generating oxidase activity
D	1903135	molecular_function	cupric ion binding
E	0005509	molecular_function	calcium ion binding
E	0016491	molecular_function	oxidoreductase activity
E	0018158	biological_process	protein oxidation
E	0043687	biological_process	post-translational protein modification
E	0046872	molecular_function	metal ion binding
E	0120147	molecular_function	formylglycine-generating oxidase activity
E	1903135	molecular_function	cupric ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 501

Chain	Residue
A	ASN194
A	ILE195
A	ASP208
A	HIS210
A	HOH623
A	HOH634

site_id	AC2
Number of Residues	3
Details	binding site for residue CU A 502

Chain	Residue
A	CYS272
A	CYS277
A	ARG279

site_id	AC3
Number of Residues	2
Details	binding site for residue CU A 503

Chain	Residue
A	HIS210
A	THR213

site_id	AC4
Number of Residues	1
Details	binding site for residue CU A 504

Chain	Residue
A	HIS81

site_id	AC5
Number of Residues	4
Details	binding site for residue CU A 505

Chain	Residue
A	HIS95
A	LEU96
A	PRO201
A	HIS202

site_id	AC6
Number of Residues	4
Details	binding site for residue IMD A 506

Chain	Residue
A	TYR276
A	ARG279
B	HIS95
B	PRO113

site_id	AC7
Number of Residues	3
Details	binding site for residue IMD B 501

Chain	Residue
B	THR79
B	HIS81
D	HIS81

site_id	AC8
Number of Residues	6
Details	binding site for residue CA B 502

Chain	Residue
B	ASN194
B	ILE195
B	ASP208
B	HIS210
B	HOH629
B	HOH631

site_id	AC9
Number of Residues	3
Details	binding site for residue CU B 503

Chain	Residue
B	CYS272
B	CYS277
B	ARG279

site_id	AD1
Number of Residues	3
Details	binding site for residue CU B 504

Chain	Residue
B	HIS210
B	THR213
B	HOH705

site_id	AD2
Number of Residues	4
Details	binding site for residue CU B 505

Chain	Residue
B	HIS95
B	LEU96
B	PRO201
B	HIS202

site_id	AD3
Number of Residues	3
Details	binding site for residue GOL C 501

Chain	Residue
C	THR23
C	GLY25
C	GLN26

site_id	AD4
Number of Residues	6
Details	binding site for residue CA C 502

Chain	Residue
C	ASN194
C	ILE195
C	ASP208
C	HIS210
C	HOH623
C	HOH649

site_id	AD5
Number of Residues	3
Details	binding site for residue CU C 503

Chain	Residue
C	CYS272
C	CYS277
C	ARG279

site_id	AD6
Number of Residues	2
Details	binding site for residue CU C 504

Chain	Residue
C	HIS81
C	HOH729

site_id	AD7
Number of Residues	4
Details	binding site for residue CU C 505

Chain	Residue
A	GLY135
A	HOH696
C	HIS210
C	HOH737

site_id	AD8
Number of Residues	2
Details	binding site for residue CU C 506

Chain	Residue
C	HIS61
C	HOH755

site_id	AD9
Number of Residues	6
Details	binding site for residue GOL C 508

Chain	Residue
C	GLY111
C	TRP234
C	LEU265
C	SER286
C	ASN288
C	ASN296

site_id	AE1
Number of Residues	5
Details	binding site for residue GOL C 509

Chain	Residue
A	ARG190
C	GLY198
C	ARG199
C	HIS273
C	SER275

site_id	AE2
Number of Residues	3
Details	binding site for residue GLY D 401

Chain	Residue
D	ASP306
D	THR308
D	SER309

site_id	AE3
Number of Residues	4
Details	binding site for residue GOL D 402

Chain	Residue
D	ARG19
D	PRO20
D	TRP155
D	ALA156

site_id	AE4
Number of Residues	6
Details	binding site for residue CA D 403

Chain	Residue
D	ASN194
D	ILE195
D	ASP208
D	HIS210
D	HOH536
D	HOH545

site_id	AE5
Number of Residues	3
Details	binding site for residue CU D 404

Chain	Residue
D	CYS272
D	CYS277
D	ARG279

site_id	AE6
Number of Residues	4
Details	binding site for residue CU D 405

Chain	Residue
D	HIS95
D	LEU96
D	PRO201
D	HIS202

site_id	AE7
Number of Residues	2
Details	binding site for residue CU D 406

Chain	Residue
D	HIS61
E	HOH561

site_id	AE8
Number of Residues	3
Details	binding site for residue CU D 407

Chain	Residue
D	ASP253
D	HIS255
D	HOH521

site_id	AE9
Number of Residues	2
Details	binding site for residue CU D 408

Chain	Residue
D	HIS210
D	HOH622

site_id	AF1
Number of Residues	4
Details	binding site for residue DTT D 409

Chain	Residue
D	SER294
E	ALA110
D	TRP115
D	ASN288

site_id	AF2
Number of Residues	6
Details	binding site for residue IMD D 410

Chain	Residue
D	TYR44
D	TYR276
D	ARG279
E	HIS95
E	PRO113
E	HIS202

site_id	AF3
Number of Residues	6
Details	binding site for residue CA E 401

Chain	Residue
E	ASN194
E	ILE195
E	ASP208
E	HIS210
E	HOH539
E	HOH560

site_id	AF4
Number of Residues	3
Details	binding site for residue CU E 402

Chain	Residue
E	CYS272
E	CYS277
E	ARG279

site_id	AF5
Number of Residues	4
Details	binding site for residue CU E 403

Chain	Residue
E	HIS210
E	HOH523
E	HOH557
E	HOH608

site_id	AF6
Number of Residues	2
Details	binding site for residue CU E 404

Chain	Residue
E	HIS81
E	HOH621

site_id	AF7
Number of Residues	2
Details	binding site for residue CU E 405

Chain	Residue
E	HIS61
E	HOH612

site_id	AF8
Number of Residues	5
Details	binding site for residue IMD E 406

Chain	Residue
B	VAL27
B	GLU64
E	ALA99
E	ARG130
E	HOH585

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:18390551, ECO:0007744\|PDB:2Q17

Chain	Residue	Details
C	ASP208
C	HIS210
D	ASN194
D	ILE195
D	ASP208
D	HIS210
E	ASN194
E	ILE195
E	ASP208
E	HIS210
A	ASN194
A	ILE195
A	ASP208
A	HIS210
B	ASN194
B	ILE195
B	ASP208
B	HIS210
C	ASN194
C	ILE195

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000305\|PubMed:25931126

Chain	Residue	Details
A	CYS272
A	CYS277
B	CYS272
B	CYS277
C	CYS272
C	CYS277
D	CYS272
D	CYS277
E	CYS272
E	CYS277

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)