2A25: Siah1 SBD

Name: PDB 2A25: Crystal structure of Siah1 SBD bound to the peptide EKPAAVVAPITTG from SIP
Published: 2005-08-09
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Crystal structure of Siah1 SBD bound to the peptide EKPAAVVAPITTG from SIP. Determined by X-ray diffraction at 2.2 Å resolution. Released 9 Aug 2005.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,320
Mol. weight: 23.01 kDa
Ligands: ZN
Released: 9 Aug 2005

Explore 2A25 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A25 contains 5 α-helices and 13 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: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	126-127	2	1
β-strand	138-139	2	1
α-helix	144-151	8
β-strand	157-159	3	2
β-strand	162-168	7	3
β-strand	177-184	8	2
β-strand	187-195	9	2
β-strand	204-211	8	2
α-helix	215-218	4
β-strand	221-229	9	3
β-strand	232-238	7	3
α-helix	239-240	2
β-strand	241-242	2	2
α-helix	248-252	5
β-strand	257-260	4	2
α-helix	261-267	7
β-strand	272-281	10	3

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	61-64	4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin ligase SIAH1	A	protein	193	Homo sapiens	Q8IUQ4 (AlphaFold model)
Calcyclin-binding protein peptide	B	protein	13		Q9HB71 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2A25_1 Ubiquitin ligase SIAH1 (chains A)
VANSVLFPCKYASSGCEITLPHTEKADHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLM
HQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFFAIV
QLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAE
NGNLGINVTISMC

Sequence of entity 2 (B), FASTA

>2A25_2 Calcyclin-binding protein peptide (chains B)
EKPAAVVAPITTG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

Structural Analysis of Siah1-Siah-interacting Protein Interactions and Insights into the Assembly of an E3 Ligase Multiprotein Complex. Santelli, E., Leone, M., Li, C. et al. J Biol Chem (2005) 280:34278-34287. DOI 10.1074/jbc.M506707200 · PubMed

Other PDB entries of the same protein (UniProt Q8IUQ4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4CA1 1.58 Å, Crystal structure of Siah1 at 1.58 A resolution.
9G0L 1.9 Å, Crystal structure of the RING-ZnF1 fragment of SIAH1
4C9Z 1.95 Å, Crystal structure of Siah1 at 1.95 A resolution
5WZZ 2.1 Å, The SIAH E3 ubiquitin ligases promote Wnt/ beta-catenin signaling through mediating…
4X3G 2.34 Å, Crystal structure of SIAH1 SINA domain in complex with a USP19 peptide
4I7D 2.4 Å, Siah1 bound to synthetic peptide (ACE)KLRPVAMVRP(PRK)VR
8HEO 2.53 Å, Crystal structure of SIAH1 SBD bound to Axin2 peptide
4I7C 2.8 Å, Siah1 mutant bound to synthetic peptide (ACE)KLRPV(23P)MVRPWVR
4I7B 3.0 Å, Siah1 bound to synthetic peptide (ACE)KLRPV(ABA)MVRPTVR

Browse structure collections

About this viewer

MolViewer shows 2A25 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.