Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6CWY

Crystal structure of SUMO E1 in complex with an allosteric inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0004839	molecular_function	ubiquitin activating enzyme activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008047	molecular_function	enzyme activator activity
C	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
C	0016567	biological_process	protein ubiquitination
C	0016874	molecular_function	ligase activity
C	0016925	biological_process	protein sumoylation
C	0019948	molecular_function	SUMO activating enzyme activity
C	0031510	cellular_component	SUMO activating enzyme complex
C	0033235	biological_process	positive regulation of protein sumoylation
C	0036211	biological_process	protein modification process
C	0043008	molecular_function	ATP-dependent protein binding
C	0044388	molecular_function	small protein activating enzyme binding
C	0046982	molecular_function	protein heterodimerization activity
C	1903955	biological_process	obsolete positive regulation of protein targeting to mitochondrion
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0008641	molecular_function	ubiquitin-like modifier activating enzyme activity
D	0016740	molecular_function	transferase activity
D	0016925	biological_process	protein sumoylation
D	0019948	molecular_function	SUMO activating enzyme activity
D	0031510	cellular_component	SUMO activating enzyme complex
D	0032183	molecular_function	SUMO binding
D	0033235	biological_process	positive regulation of protein sumoylation
D	0044388	molecular_function	small protein activating enzyme binding
D	0044390	molecular_function	ubiquitin-like protein conjugating enzyme binding
D	0046872	molecular_function	metal ion binding
D	0046982	molecular_function	protein heterodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue GOL C 401

Chain	Residue
C	HIS162
C	PRO288
C	PHE291
C	TYR294

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL C 402

Chain	Residue
C	ILE115
C	VAL42
C	ASP67
C	HIS68
C	GLU69
C	ASP114

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN D 701

Chain	Residue
D	CYS158
D	CYS161
D	CYS441
D	CYS444

site_id	AC4
Number of Residues	4
Details	binding site for residue MG D 702

Chain	Residue
D	ILE96
D	ASN98
D	TYR101
D	HIS124

site_id	AC5
Number of Residues	6
Details	binding site for residue SO4 D 703

Chain	Residue
D	ARG176
D	GLU205
D	PRO208
D	ASP209
D	ARG210
D	ALA211

site_id	AC6
Number of Residues	5
Details	binding site for residue SO4 D 704

Chain	Residue
D	ARG119
D	PRO165
D	THR166
D	ARG168
D	SER378

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 D 705

Chain	Residue
D	GLN74
D	LYS77
D	ALA91

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 D 706

Chain	Residue
D	PHE417
D	ASN419
D	VAL430

site_id	AC9
Number of Residues	8
Details	binding site for residue FHJ D 707

Chain	Residue
C	GLN79
D	CYS30
D	GLU31
D	LYS34
D	ALA76
D	SER79
D	VAL80
D	PHE83

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
D	LYS404-GLN412

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

Chain	Residue	Details
D	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	13
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":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
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_FI6
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_FI7
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_FI8
Number of Residues	3
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_FI9
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_FI10
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_FI11
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate"}

Chain

Residue

Details

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