2IYC: SENP1 native structure

SENP1 native structure. Determined by X-ray diffraction at 2.45 Å resolution. Released 8 Aug 2006.

Method: X-ray diffraction
Resolution: 2.45 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,872
Mol. weight: 53.86 kDa
Released: 8 Aug 2006

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

Secondary structure: helices and β-sheets

2IYC contains 35 α-helices and 20 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: 17 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	425-434	10
β-strand	443-447	5	1
β-strand	450-453	4	1
α-helix	454-458	5
α-helix	464-466	3
α-helix	468-481	14
β-strand	482	1	2
β-strand	484	1	2
α-helix	488-489	2
β-strand	490-492	3	3
α-helix	493-494	2
α-helix	496-504	9
α-helix	506-508	3
α-helix	510-513	4
α-helix	518-520	3
β-strand	523-530	8	3
β-strand	533-540	8	3
β-strand	545-549	5	3
α-helix	557-575	19
β-strand	585-588	4	3
α-helix	589-590	2
α-helix	595-597	3
β-strand	599	1	4
α-helix	600-602	3
α-helix	603-615	13
α-helix	624-626	3
α-helix	627-640	14

Chain B: 18 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	420-422	3
α-helix	425-434	10
β-strand	443-447	5	5
β-strand	450-453	4	5
α-helix	454-458	5
α-helix	464-467	4
α-helix	468-481	14
β-strand	482	1	6
β-strand	484	1	6
α-helix	488-489	2
β-strand	490-492	3	7
α-helix	493-494	2
α-helix	496-504	9
α-helix	506-508	3
α-helix	510-513	4
α-helix	518-520	3
β-strand	523-530	8	7
β-strand	533-540	8	7
β-strand	545-549	5	7
β-strand	555	1	4
α-helix	557-575	19
β-strand	585-588	4	7
α-helix	589-590	2
α-helix	595-597	3
α-helix	600-602	3
α-helix	603-615	13
α-helix	624-626	3
α-helix	627-640	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sentrin-specific protease 1	A, B	protein	226	HOMO SAPIENS	Q9P0U3 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2IYC_1 SENTRIN-SPECIFIC PROTEASE 1 (chains A, B)
EFPEITEEMEKEIKNVFRNGNQDEVLSEAFRLTITRKDIQTLNHLNWLNDEIINFYMNML
MERSKEKGLPSVHAFNTFFFTKLKTAGYQAVKRWTKKVDVFSVDILLVPIHLGVHWCLAV
VDFRKKNITYYDSMGGINNEACRILLQYLKQESIDKKRKEFDTNGWQLFSKKSQEIPQQM
NGSDCGMFACKYADCITKDRPINFTQQHMPYFRKRMVWEILHRKLL

Primary citation

Senp1 Native Structure. Dong, C., Naismith, J.H. To be published.

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…
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
2CKH 3.2 Å, SENP1-SUMO2 complex
2IYD 3.2 Å, SENP1 covalent complex with SUMO-2

Browse structure collections

About this viewer

MolViewer shows 2IYC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.