2CKH: SENP1-SUMO2 complex

SENP1-SUMO2 complex. Determined by X-ray diffraction at 3.2 Å resolution. Released 26 Apr 2006.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 2,515
Mol. weight: 35.87 kDa
Released: 26 Apr 2006

Explore 2CKH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CKH contains 15 α-helices and 14 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	420-422	3
α-helix	425-435	11
β-strand	445	1	1
β-strand	452	1	1
α-helix	454-458	5
α-helix	464-465	2
β-strand	466-467	2	2
α-helix	468-481	14
β-strand	490-492	3	3
α-helix	496-504	9
α-helix	506-509	4
α-helix	518-520	3
β-strand	523-529	7	3
β-strand	534-540	7	3
β-strand	545-549	5	3
α-helix	557-574	18
β-strand	585-588	4	3
α-helix	602-614	13
α-helix	617-619	3
α-helix	625-639	15

Chain B: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	16-23	8	4
β-strand	27-34	8	4
α-helix	40-48	9
β-strand	57-61	5	4
β-strand	64-65	2	4
α-helix	66	1
α-helix	72-75	4
β-strand	81-87	7	4
β-strand	90-91	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sentrin-specific protease 1	A	protein	225	HOMO SAPIENS	Q9P0U3 (AlphaFold model)
Small ubiquitin-related modifier 2	B	protein	79	HOMO SAPIENS	P61956 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2CKH_1 SENTRIN-SPECIFIC PROTEASE 1 (chains A)
EFPEITEEMEKEIKNVFRNGNQDEVLSEAFRLTITRKDIQTLNHLNWLNDEIINFYMNML
MERSKEKGLPSVHAFNTFFFTKLKTAGYQAVKRWTKKVDVFSVDILLVPIHLGVHWCLAV
VDFRKKNITYYDSMGGINNEACRILLQYLKQESIDKKRKEFDTNGWQLFSKKSQIPQQMN
GSDCGMFACKYADCITKDRPINFTQQHMPYFRKRMVWEILHRKLL

Sequence of entity 2 (B), FASTA

>2CKH_2 SMALL UBIQUITIN-RELATED MODIFIER 2 (chains B)
NDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPA
QLEMEDEDTIDVFQQQTGG

Primary citation

The Structure of Senp1-Sumo-2 Complex Suggests a Structural Basis for Discrimination between Sumo Paralogues During Processing. Shen, L.N., Dong, C., Liu, H. et al. Biochem J (2006) 397:279. DOI 10.1042/BJ20052030 · PubMed

Other PDB entries of the same protein (UniProt Q9P0U3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2XPH 2.4 Å, Crystal structure of human SENP1 with the bound cobalt
2CKG 2.45 Å, The structure of SENP1 SUMO-2 co-complex suggests a structural basis for discrimination…
2IYC 2.45 Å, SENP1 native structure
2XRE 2.45 Å, Detection of cobalt in previously unassigned human SENP1 structure
2IY1 2.46 Å, SENP1 (mutant) full length SUMO1
6NNQ 2.62 Å, Non-covalent structure of SENP1 in complex with SUMO2
2IY0 2.77 Å, SENP1 (mutant) SUMO1 RanGAP
2G4D 2.8 Å, Crystal structure of human SENP1 mutant (C603S) in complex with SUMO-1
2IYD 3.2 Å, SENP1 covalent complex with SUMO-2

Browse structure collections

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