6GWJ

Human OSGEP / LAGE3 / GON7 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000408	cellular_component	EKC/KEOPS complex
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0008033	biological_process	tRNA processing
B	0008150	biological_process	biological_process
B	0016604	cellular_component	nuclear body
B	0070525	biological_process	tRNA threonylcarbamoyladenosine metabolic process
D	0000408	cellular_component	EKC/KEOPS complex
D	0002949	biological_process	tRNA threonylcarbamoyladenosine modification
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005730	cellular_component	nucleolus
D	0005829	cellular_component	cytosol
K	0000408	cellular_component	EKC/KEOPS complex
K	0002949	biological_process	tRNA threonylcarbamoyladenosine modification
K	0005515	molecular_function	protein binding
K	0005634	cellular_component	nucleus
K	0005654	cellular_component	nucleoplasm
K	0005737	cellular_component	cytoplasm
K	0005829	cellular_component	cytosol
K	0006400	biological_process	tRNA modification
K	0008033	biological_process	tRNA processing
K	0016746	molecular_function	acyltransferase activity
K	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
K	0046872	molecular_function	metal ion binding
K	0061711	molecular_function	N(6)-L-threonylcarbamoyladenine synthase activity
K	0070525	biological_process	tRNA threonylcarbamoyladenosine metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue GOL B 201

Chain	Residue
B	PRO88
B	HIS89
B	GLN90
B	ARG91
B	VAL92
B	HOH327
K	SER209
K	PHE210
K	ASP213

---

site_id	AC2
Number of Residues	7
Details	binding site for residue GOL D 201

Chain	Residue
B	GLN135
D	ASP28
D	PHE30
D	HOH302
D	HOH304
D	HOH305
K	ARG312

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site_id	AC3
Number of Residues	5
Details	binding site for residue TRS K 401

Chain	Residue
D	ASP42
D	HOH301
K	GLU143
K	HIS144
K	ASP335

---

site_id	AC4
Number of Residues	7
Details	binding site for residue MG K 402

Chain	Residue
K	HIS109
K	HIS113
K	TYR130
K	ASP294
K	HOH503
K	HOH528
K	HOH555

---

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL K 403

Chain	Residue
B	ALA86
K	GLY83
K	ALA84
K	VAL320
K	GLN322
K	HOH608

---

site_id	AC6
Number of Residues	6
Details	binding site for residue GOL K 404

Chain	Residue
B	ARG132
K	ALA51
K	ARG308
K	HOH527
K	HOH534
K	HOH603

---

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL K 405

Chain	Residue
K	ASN12
K	LYS13
K	THR31
K	ASN172
K	PRO174
K	SER175
K	PRO176

---

site_id	AC8
Number of Residues	6
Details	binding site for residue PEG K 406

Chain	Residue
K	GLY22
K	LYS23
K	VAL24
K	LEU119
K	ILE120
K	HOH533

---

site_id	AC9
Number of Residues	2
Details	binding site for residue PEG K 407

Chain	Residue
B	ARG143
K	GLN98

---

site_id	AD1
Number of Residues	11
Details	binding site for residue PEG K 408

Chain	Residue
D	GLN31
D	HOH308
K	LYS78
K	GLY106
K	HIS311
K	ARG312
K	THR313
K	PRO314
K	ASP317
K	TYR324
K	HOH611

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Functional Information from PROSITE/UniProt

site_id	PS01016
Number of Residues	21
Details	GLYCOPROTEASE Glycoprotease family signature. RTvaqlWNkPlVgvnHciGHI

Chain	Residue	Details
K	ARG94-ILE114

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03180

Chain	Residue	Details
K	HIS109
K	HIS113
K	TYR130
K	ASP162
K	GLY177
K	GLU181
K	ASN266
K	ASP294

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