Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6O82

S. pombe ubiquitin E1 complex with a ubiquitin-AMP mimic

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004839	molecular_function	ubiquitin activating enzyme activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0006974	biological_process	DNA damage response
A	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
A	0016567	biological_process	protein ubiquitination
A	0016874	molecular_function	ligase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0036211	biological_process	protein modification process
C	0000287	molecular_function	magnesium ion binding
C	0004839	molecular_function	ubiquitin activating enzyme activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0006974	biological_process	DNA damage response
C	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
C	0016567	biological_process	protein ubiquitination
C	0016874	molecular_function	ligase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0036211	biological_process	protein modification process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 1101

Chain	Residue
A	ASP537
A	POP1103
A	HOH1262
A	HOH1293
B	JZU101

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 1102

Chain	Residue
A	HOH1230
A	HOH1246
A	ASP465
A	POP1103
A	HOH1217
A	HOH1225

site_id	AC3
Number of Residues	17
Details	binding site for residue POP A 1103

Chain	Residue
A	ARG22
A	ASP465
A	ASN471
A	ARG474
A	GLN475
A	LYS487
A	ASP537
A	MG1101
A	MG1102
A	HOH1217
A	HOH1220
A	HOH1225
A	HOH1230
A	HOH1262
A	HOH1293
A	HOH1313
B	JZU101

site_id	AC4
Number of Residues	4
Details	binding site for residue POP A 1104

Chain	Residue
A	GLY28
A	HIS29
A	GLU30
A	HOH1222

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 A 1105

Chain	Residue
A	ARG986
A	HIS988
A	VAL990
A	HOH1202
A	HOH1204

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 A 1106

Chain	Residue
A	HIS147
A	GLY167
A	GLU168
A	ASN169

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 A 1107

Chain	Residue
A	THR14
A	ILE15
A	HIS29

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 A 1108

Chain	Residue
A	ASN39
A	THR65
A	PHE123

site_id	AC9
Number of Residues	2
Details	binding site for residue SO4 A 1109

Chain	Residue
A	LYS216
A	GLY217

site_id	AD1
Number of Residues	3
Details	binding site for residue EDO A 1110

Chain	Residue
A	ASP840
A	ARG841
A	PHE842

site_id	AD2
Number of Residues	18
Details	binding site for residue JZU B 101

Chain	Residue
A	ALA437
A	ASP463
A	ASP465
A	ARG474
A	GLN475
A	LYS487
A	ARG512
A	VAL513
A	ALA535
A	LEU536
A	ASP537
A	ASN538
A	ALA541
A	MG1101
A	POP1103
A	HOH1293
B	GLY76
B	HOH210

site_id	AD3
Number of Residues	5
Details	binding site for residue MG C 1101

Chain	Residue
C	ASP537
C	POP1103
C	HOH1203
C	HOH1210
D	JZU101

site_id	AD4
Number of Residues	3
Details	binding site for residue MG C 1102

Chain	Residue
C	ASP465
C	GLU468
C	POP1103

site_id	AD5
Number of Residues	12
Details	binding site for residue POP C 1103

Chain	Residue
C	ARG22
C	ASP465
C	ASN471
C	ARG474
C	GLN475
C	LYS487
C	ASP537
C	MG1101
C	MG1102
C	HOH1203
C	HOH1210
D	JZU101

site_id	AD6
Number of Residues	2
Details	binding site for residue SO4 C 1104

Chain	Residue
C	TYR544
C	ARG547

site_id	AD7
Number of Residues	4
Details	binding site for residue SO4 C 1105

Chain	Residue
C	GLU518
C	ARG986
C	LYS987
C	HIS988

site_id	AD8
Number of Residues	2
Details	binding site for residue EDO C 1106

Chain	Residue
C	HIS29
C	PHE842

Functional Information from PROSITE/UniProt

site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KskIqDkegIPpdqQrLIFaGkqleD

Chain	Residue	Details
B	LYS27-ASP52

site_id	PS00865
Number of Residues	9
Details	UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PICTLKnFP

Chain	Residue	Details
A	PRO591-PRO599

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Chain	Residue	Details
B	LYS6
B	LYS11
B	LYS27
B	LYS33
D	LYS6
D	LYS11
D	LYS27
D	LYS33

site_id	SWS_FT_FI2
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255\|PROSITE-ProRule:PRU00214

Chain	Residue	Details
A	ARG22
C	LYS487
C	VAL513
C	ASP537
B	GLY76
A	ASP463
D	GLY76
A	VAL513
A	ASP537
C	ARG22
C	ALA437
C	ASP463

site_id	SWS_FT_FI3
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250

Chain	Residue	Details
B	LYS29
B	LYS48
B	LYS63
D	LYS29
D	LYS48
D	LYS63

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