Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KYD

Human SUMO E1~SUMO1-AMP tetrahedral intermediate mimic

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004839	molecular_function	ubiquitin activating enzyme activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0008047	molecular_function	enzyme activator activity
A	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
A	0016567	biological_process	protein ubiquitination
A	0016874	molecular_function	ligase activity
A	0016925	biological_process	protein sumoylation
A	0019948	molecular_function	SUMO activating enzyme activity
A	0031510	cellular_component	SUMO activating enzyme complex
A	0033235	biological_process	positive regulation of protein sumoylation
A	0036211	biological_process	protein modification process
A	0043008	molecular_function	ATP-dependent protein binding
A	0044388	molecular_function	small protein activating enzyme binding
A	0046982	molecular_function	protein heterodimerization activity
A	1903955	biological_process	positive regulation of protein targeting to mitochondrion
B	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
B	0016925	biological_process	protein sumoylation
B	0019948	molecular_function	SUMO activating enzyme activity
D	0001741	cellular_component	XY body
D	0003723	molecular_function	RNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005643	cellular_component	nuclear pore
D	0005654	cellular_component	nucleoplasm
D	0005730	cellular_component	nucleolus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0006281	biological_process	DNA repair
D	0006355	biological_process	regulation of DNA-templated transcription
D	0008076	cellular_component	voltage-gated potassium channel complex
D	0008134	molecular_function	transcription factor binding
D	0010621	biological_process	obsolete negative regulation of transcription by transcription factor localization
D	0015459	molecular_function	potassium channel regulator activity
D	0016020	cellular_component	membrane
D	0016604	cellular_component	nuclear body
D	0016605	cellular_component	PML body
D	0016607	cellular_component	nuclear speck
D	0016925	biological_process	protein sumoylation
D	0019899	molecular_function	enzyme binding
D	0030578	biological_process	PML body organization
D	0031334	biological_process	positive regulation of protein-containing complex assembly
D	0031386	molecular_function	protein tag activity
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0031647	biological_process	regulation of protein stability
D	0031965	cellular_component	nuclear membrane
D	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
D	0032880	biological_process	regulation of protein localization
D	0034605	biological_process	cellular response to heat
D	0042308	biological_process	negative regulation of protein import into nucleus
D	0043392	biological_process	negative regulation of DNA binding
D	0043433	biological_process	negative regulation of DNA-binding transcription factor activity
D	0044388	molecular_function	small protein activating enzyme binding
D	0044389	molecular_function	ubiquitin-like protein ligase binding
D	0045759	biological_process	negative regulation of action potential
D	0045892	biological_process	negative regulation of DNA-templated transcription
D	0050821	biological_process	protein stabilization
D	0060021	biological_process	roof of mouth development
D	0071276	biological_process	cellular response to cadmium ion
D	0086004	biological_process	regulation of cardiac muscle cell contraction
D	0090204	biological_process	protein localization to nuclear pore
D	0097165	cellular_component	nuclear stress granule
D	0098978	cellular_component	glutamatergic synapse
D	0099523	cellular_component	presynaptic cytosol
D	0099524	cellular_component	postsynaptic cytosol
D	0141109	molecular_function	transporter activator activity
D	1901017	biological_process	negative regulation of potassium ion transmembrane transporter activity
D	1902260	biological_process	negative regulation of delayed rectifier potassium channel activity
D	1903169	biological_process	regulation of calcium ion transmembrane transport
D	1990381	molecular_function	ubiquitin-specific protease binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 347

Chain	Residue
A	PHE159
A	GLY163
A	TYR164
A	ASP239
A	LEU242
A	LEU243
A	HOH414

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 348

Chain	Residue
A	ARG98
B	GLN82
A	ARG83
A	GLU97

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 550

Chain	Residue
B	CYS158
B	CYS161
B	CYS441
B	CYS444

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE VMX D 97

Chain	Residue
B	GLY24
B	GLY27
B	ILE28
B	ASP48
B	LEU49
B	ASP50
B	LYS72
B	ASP94
B	SER95
B	ILE96
B	ALA115
B	LEU116
B	ASP117
B	ASN118
B	THR141
B	CYS173
B	THR174
B	ARG176
B	HOH614
D	GLY96

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 98

Chain	Residue
A	ARG235
B	ARG425
B	HOH651
D	GLU67

Functional Information from PROSITE/UniProt

site_id	PS00536
Number of Residues	9
Details	UBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KILSGKIdQ

Chain	Residue	Details
B	LYS404-GLN412

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

Chain	Residue	Details
B	PRO171-PRO179

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10132","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20164921","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15660128","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

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)"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	3
Details	Region: {"description":"(Microbial infection) Interaction with Tula hantavirus","evidences":[{"source":"PubMed","id":"12606074","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Site: {"description":"Interaction with PIAS2"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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