Brand  (β version)

PDB ID: 3KYC

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Ligands
Code Name Style Show Link
JZU 5'-deoxy-5'-(sulfamoylamino)adenosine PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Glycosylation
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Modification
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Structure summary

Code : 3KYC   PDBj   RCSB PDB   PDBe
Header : LIGASE
Title : Human SUMO E1 complex with a SUMO1-AMP mimic
Release Data : 2010-02-16
Compound :
mol_id molecule chains synonym
1 SUMO-activating enzyme subunit 1 A Ubiquitin-like 1-activating enzyme E1A
mol_id molecule chains synonym
2 SUMO-activating enzyme subunit 2 B Ubiquitin-like 1-activating enzyme E1B, Anthracycline-associated resistance ARX
ec: 6.3.2.-
mol_id molecule chains synonym
3 Small ubiquitin-related modifier 1 D SUMO-1, Sentrin, Ubiquitin-like protein SMT3C, SMT3 homolog 3, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein UBL1, GAP-modifying protein 1, GMP1
fragment: UNP residues 1-97
mutation: T95C
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: AOS1, SAE1, SUA1, UBLE1A
expression_system_strain: BL21 DE3 CP RIL
expression_system_vector_type: PLASMID
expression_system_plasmid: pET-15b
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: HRIHFB2115, SAE2, UBA2, UBLE1B
expression_system_strain: BL21 DE3 CP RIL
expression_system_vector_type: PLASMID
expression_system_plasmid: pET28b
mol_id organism_scientific organism_common expression_system
3 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: OK/SW-cl.43, SMT3C, SMT3H3, SUMO1, UBL1
expression_system_strain: BL21 DE3 CP RIL
expression_system_vector_type: PLASMID
expression_system_plasmid: pTXB1
Authors : Lima, C.D.
Keywords : E1, SUMO, UBIQUITIN, THIOESTER, ADENYLATION, INHIBITOR, ACYL-ADENYLATE INTERMEDIATE, Acetylation, Ligase, Nucleus, Phosphoprotein, Ubl conjugation pathway, ATP-binding, Nucleotide-binding, Polymorphism, Cytoplasm, Isopeptide bond, Membrane
Exp. method : X-RAY DIFFRACTION ( 2.450 Å )
Citation :

Active site remodelling accompanies thioester bond formation in the SUMO E1.

Olsen, S.K.,Capili, A.D.,Lu, X.  et al.
(2010)  Nature  463 : 906 - 912

PubMed: 20164921
DOI: 10.1038/nature08765

Reaction

Chain : A
UniProt : Q9UBE0 (SAE1_HUMAN)
Reaction : -
Chain : B
UniProt : Q9UBT2 (SAE2_HUMAN)
Reaction : -
Chain : D
UniProt : P63165 (SUMO1_HUMAN)
Reaction : -