Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3V62

Structure of the S. cerevisiae Srs2 C-terminal domain in complex with PCNA conjugated to SUMO on lysine 164

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000278	biological_process	mitotic cell cycle
B	0000710	biological_process	meiotic mismatch repair
B	0000781	cellular_component	chromosome, telomeric region
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005657	cellular_component	replication fork
B	0006260	biological_process	DNA replication
B	0006272	biological_process	leading strand elongation
B	0006273	biological_process	lagging strand elongation
B	0006275	biological_process	regulation of DNA replication
B	0006281	biological_process	DNA repair
B	0006289	biological_process	nucleotide-excision repair
B	0006298	biological_process	mismatch repair
B	0006301	biological_process	postreplication repair
B	0007064	biological_process	mitotic sister chromatid cohesion
B	0019985	biological_process	translesion synthesis
B	0030337	molecular_function	DNA polymerase processivity factor activity
B	0030466	biological_process	silent mating-type cassette heterochromatin formation
B	0031509	biological_process	subtelomeric heterochromatin formation
B	0034087	biological_process	establishment of mitotic sister chromatid cohesion
B	0035753	biological_process	maintenance of DNA trinucleotide repeats
B	0042802	molecular_function	identical protein binding
B	0043626	cellular_component	PCNA complex
B	0045739	biological_process	positive regulation of DNA repair
B	0045740	biological_process	positive regulation of DNA replication
B	0051054	biological_process	positive regulation of DNA metabolic process
B	0070987	biological_process	error-free translesion synthesis
E	0000278	biological_process	mitotic cell cycle
E	0000710	biological_process	meiotic mismatch repair
E	0000781	cellular_component	chromosome, telomeric region
E	0003677	molecular_function	DNA binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005657	cellular_component	replication fork
E	0006260	biological_process	DNA replication
E	0006272	biological_process	leading strand elongation
E	0006273	biological_process	lagging strand elongation
E	0006275	biological_process	regulation of DNA replication
E	0006281	biological_process	DNA repair
E	0006289	biological_process	nucleotide-excision repair
E	0006298	biological_process	mismatch repair
E	0006301	biological_process	postreplication repair
E	0007064	biological_process	mitotic sister chromatid cohesion
E	0019985	biological_process	translesion synthesis
E	0030337	molecular_function	DNA polymerase processivity factor activity
E	0030466	biological_process	silent mating-type cassette heterochromatin formation
E	0031509	biological_process	subtelomeric heterochromatin formation
E	0034087	biological_process	establishment of mitotic sister chromatid cohesion
E	0035753	biological_process	maintenance of DNA trinucleotide repeats
E	0042802	molecular_function	identical protein binding
E	0043626	cellular_component	PCNA complex
E	0045739	biological_process	positive regulation of DNA repair
E	0045740	biological_process	positive regulation of DNA replication
E	0051054	biological_process	positive regulation of DNA metabolic process
E	0070987	biological_process	error-free translesion synthesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NEQ B 301

Chain	Residue
B	GLY18
B	PHE19
B	CYS22
B	VAL48

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NEQ B 302

Chain	Residue
B	LYS77
B	CYS81
B	TYR114
E	GLN153
E	LEU154

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 303

Chain	Residue
B	SER138
B	LYS196
B	ARG224

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 304

Chain	Residue
B	LYS146
B	ARG149

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NEQ E 301

Chain	Residue
E	GLY18
E	PHE19
E	CYS22

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NEQ E 302

Chain	Residue
B	GLN153
B	LEU154
E	LYS77
E	CYS81
E	TYR114

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 303

Chain	Residue
E	SER138
E	LYS196
E	ARG224
E	HOH408

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 E 304

Chain	Residue
E	LYS146
E	ARG149

Functional Information from PROSITE/UniProt

site_id	PS00293
Number of Residues	19
Details	PCNA_2 Proliferating cell nuclear antigen signature 2. RCDHpvtLgmdLtSLsKIL

Chain	Residue	Details
B	ARG61-LEU79

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

Chain	Residue	Details
B	GLY34-PHE57

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	38
Details	DNA_BIND: DNA_BIND => ECO:0000255

Chain	Residue	Details
B	ARG61-ARG80
E	ARG61-ARG80
D	GLY98

site_id	SWS_FT_FI2
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269\|PubMed:15166219

Chain	Residue	Details
B	GLY127
E	GLY127

site_id	SWS_FT_FI3
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:12226657

Chain	Residue	Details
B	LYS164
E	LYS164

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