5JNE

E2-SUMO-Siz1 E3-SUMO-PCNA complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008270	molecular_function	zinc ion binding
B	0000022	biological_process	mitotic spindle elongation
B	0000166	molecular_function	nucleotide binding
B	0000794	cellular_component	condensed nuclear chromosome
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005694	cellular_component	chromosome
B	0016740	molecular_function	transferase activity
B	0016925	biological_process	protein sumoylation
B	0019789	molecular_function	SUMO transferase activity
B	0051301	biological_process	cell division
B	0061656	molecular_function	SUMO conjugating enzyme activity
D	0000278	biological_process	mitotic cell cycle
D	0000710	biological_process	meiotic mismatch repair
D	0000781	cellular_component	chromosome, telomeric region
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005657	cellular_component	replication fork
D	0006260	biological_process	DNA replication
D	0006272	biological_process	leading strand elongation
D	0006273	biological_process	lagging strand elongation
D	0006275	biological_process	regulation of DNA replication
D	0006289	biological_process	nucleotide-excision repair
D	0006298	biological_process	mismatch repair
D	0006301	biological_process	DNA damage tolerance
D	0006974	biological_process	DNA damage response
D	0007064	biological_process	mitotic sister chromatid cohesion
D	0019985	biological_process	translesion synthesis
D	0030337	molecular_function	DNA polymerase processivity factor activity
D	0030466	biological_process	silent mating-type cassette heterochromatin formation
D	0031509	biological_process	subtelomeric heterochromatin formation
D	0034087	biological_process	establishment of mitotic sister chromatid cohesion
D	0035753	biological_process	maintenance of DNA trinucleotide repeats
D	0042802	molecular_function	identical protein binding
D	0043626	cellular_component	PCNA complex
D	0045739	biological_process	positive regulation of DNA repair
D	0045740	biological_process	positive regulation of DNA replication
D	0051054	biological_process	positive regulation of DNA metabolic process
D	0070987	biological_process	error-free translesion synthesis
E	0008270	molecular_function	zinc ion binding
F	0000022	biological_process	mitotic spindle elongation
F	0000166	molecular_function	nucleotide binding
F	0000794	cellular_component	condensed nuclear chromosome
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0005694	cellular_component	chromosome
F	0016740	molecular_function	transferase activity
F	0016925	biological_process	protein sumoylation
F	0019789	molecular_function	SUMO transferase activity
F	0051301	biological_process	cell division
F	0061656	molecular_function	SUMO conjugating enzyme activity
H	0000278	biological_process	mitotic cell cycle
H	0000710	biological_process	meiotic mismatch repair
H	0000781	cellular_component	chromosome, telomeric region
H	0003677	molecular_function	DNA binding
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005657	cellular_component	replication fork
H	0006260	biological_process	DNA replication
H	0006272	biological_process	leading strand elongation
H	0006273	biological_process	lagging strand elongation
H	0006275	biological_process	regulation of DNA replication
H	0006289	biological_process	nucleotide-excision repair
H	0006298	biological_process	mismatch repair
H	0006301	biological_process	DNA damage tolerance
H	0006974	biological_process	DNA damage response
H	0007064	biological_process	mitotic sister chromatid cohesion
H	0019985	biological_process	translesion synthesis
H	0030337	molecular_function	DNA polymerase processivity factor activity
H	0030466	biological_process	silent mating-type cassette heterochromatin formation
H	0031509	biological_process	subtelomeric heterochromatin formation
H	0034087	biological_process	establishment of mitotic sister chromatid cohesion
H	0035753	biological_process	maintenance of DNA trinucleotide repeats
H	0042802	molecular_function	identical protein binding
H	0043626	cellular_component	PCNA complex
H	0045739	biological_process	positive regulation of DNA repair
H	0045740	biological_process	positive regulation of DNA replication
H	0051054	biological_process	positive regulation of DNA metabolic process
H	0070987	biological_process	error-free translesion synthesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 601

Chain	Residue
A	CYS377
A	HIS379
A	CYS400
A	CYS403

---

site_id	AC2
Number of Residues	4
Details	binding site for residue GOL A 602

Chain	Residue
A	ILE175
A	HIS176
A	PHE177
A	TYR309

---

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 603

Chain	Residue
A	TRP398
A	LEU409
A	GLU410
A	LYS178

---

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 604

Chain	Residue
A	ALA333
A	THR334
A	LYS373
A	CYS377
A	LYS378
A	HIS379

---

site_id	AC5
Number of Residues	7
Details	binding site for residue 6LN B 201

Chain	Residue
B	CYS93
B	LEU94
B	ASN98
B	GLN101
C	GLY97
C	GLY98
D	CYS164

---

site_id	AC6
Number of Residues	5
Details	binding site for residue GOL D 301

Chain	Residue
A	LYS471
D	GLU81
D	ASP86
D	ASP105
D	ALA112

---

site_id	AC7
Number of Residues	3
Details	binding site for residue GOL D 302

Chain	Residue
A	ARG488
D	GLU104
D	THR106

---

site_id	AC8
Number of Residues	5
Details	binding site for residue GOL D 303

Chain	Residue
A	LYS302
D	GLN132
D	THR136
D	GLU198
D	ASP200

---

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN E 601

Chain	Residue
E	CYS377
E	HIS379
E	CYS400
E	CYS403

---

site_id	AD1
Number of Residues	5
Details	binding site for residue GOL E 602

Chain	Residue
E	ILE175
E	HIS176
E	PHE177
E	ILE185
E	TYR309

---

site_id	AD2
Number of Residues	3
Details	binding site for residue GOL E 603

Chain	Residue
E	LYS178
E	TRP398
E	GLU410

---

site_id	AD3
Number of Residues	8
Details	binding site for residue 6LN F 201

Chain	Residue
F	CYS93
F	LEU94
F	ASN98
F	GLN101
G	ILE96
G	GLY97
G	GLY98
H	CYS164

---

site_id	AD4
Number of Residues	6
Details	binding site for residue GOL H 301

Chain	Residue
E	LYS471
H	GLU81
H	ASP86
H	PHE103
H	ASP105
H	ALA112

---

site_id	AD5
Number of Residues	5
Details	binding site for residue GOL H 302

Chain	Residue
E	LYS302
H	TYR133
H	THR136
H	GLU198
H	ASP200

---

site_id	AD6
Number of Residues	21
Details	binding site for Di-peptide GLY G 98 and LYS F 129

Chain	Residue
F	PRO84
F	VAL86
F	TYR87
F	PRO88
F	CYS93
F	LEU94
F	SER95
F	ILE96
F	LEU97
F	GLU99
F	ASP100
F	GLN101
F	ASP102
F	TRP103
F	SER127
F	PRO128
F	GLN130
F	6LN201
G	GLY97
H	THR166
H	LYS183

---

Functional Information from PROSITE/UniProt

site_id	PS00183
Number of Residues	16
Details	UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNVyps.GtICLsiL

Chain	Residue	Details
B	TYR82-LEU97

---

site_id	PS01251
Number of Residues	24
Details	PCNA_1 Proliferating cell nuclear antigen signature 1. GIiAqAVDdSRVlLVsLeIgveaF

Chain	Residue	Details
D	GLY34-PHE57

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	174
Details	Zinc finger: {"description":"SP-RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00452","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00452","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	152
Details	Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	38
Details	DNA binding: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"15166219","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"12226657","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---