4I7D: Siah1

Siah1 bound to synthetic peptide (ACE)KLRPVAMVRP(PRK)VR. Determined by X-ray diffraction at 2.4 Å resolution. Released 14 Aug 2013.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Homo sapiens, Drosophila melanogaster
Chains: 4
Atoms: 3,342
Mol. weight: 47.6 kDa
Ligands: ZN
Released: 14 Aug 2013

Explore 4I7D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4I7D contains 22 α-helices and 36 β-strands across 4 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: 9 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	96-97	2	1
α-helix	99-103	5
β-strand	108-109	2	1
α-helix	111-113	3
α-helix	114-120	7
α-helix	125	1
β-strand	126-127	2	2
β-strand	138-139	2	2
α-helix	141-151	11
β-strand	156-159	4	3
β-strand	162-167	6	4
β-strand	176-184	9	3
β-strand	187-196	10	3
β-strand	204-211	8	3
α-helix	215-218	4
β-strand	221-229	9	4
β-strand	232-238	7	4
α-helix	239-240	2
β-strand	241-242	2	3
α-helix	248-252	5
β-strand	257-260	4	3
α-helix	261-267	7
β-strand	269	1	5
β-strand	272	1	5
β-strand	273-281	9	4

Chain B: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	117-120	4	4
β-strand	123-124	2	3

Chain C: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	95	1
β-strand	96-97	2	6
α-helix	98	1
α-helix	101-103	3
β-strand	108-109	2	6
α-helix	114-120	7
α-helix	125	1
β-strand	126-127	2	7
α-helix	128	1
β-strand	138-139	2	7
α-helix	141-143	3
α-helix	144-151	8
β-strand	157-159	3	8
β-strand	162-167	6	4
β-strand	176-184	9	8
β-strand	187-197	11	8
β-strand	203-211	9	8
α-helix	215-218	4
β-strand	221-229	9	4
β-strand	232-238	7	4
α-helix	239-240	2
β-strand	241-242	2	8
α-helix	248-252	5
β-strand	257-260	4	8
α-helix	261-267	7
β-strand	269	1	9
β-strand	272	1	9
β-strand	273-281	9	4

Chain D: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	117-120	4	4
α-helix	121-122	2
β-strand	123-124	2	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase SIAH1	A, C	protein	196	Homo sapiens	Q8IUQ4 (AlphaFold model)
Protein phyllopod	B, D	protein	14	Drosophila melanogaster	Q27934 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4I7D_1 E3 ubiquitin-protein ligase SIAH1 (chains A, C)
GSHVANSVLFPCKYASSGCEITLPHTEKADHEELCEFRPYSCPCPGASCKWQGSLDAVMP
HLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFF
AIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQL
FAENGNLGINVTISMC

Sequence of entity 2 (B, D), FASTA

>4I7D_2 Protein phyllopod (chains B, D)
XKLRPVAMVRPXVR

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Water and common crystallization additives (MPD) are not listed.

Primary citation

Structure-based design of covalent siah inhibitors. Stebbins, J.L., Santelli, E., Feng, Y. et al. Chem Biol (2013) 20:973-982. DOI 10.1016/j.chembiol.2013.06.008 · 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…
2A25 2.2 Å, Crystal structure of Siah1 SBD bound to the peptide EKPAAVVAPITTG from SIP
4X3G 2.34 Å, Crystal structure of SIAH1 SINA domain in complex with a USP19 peptide
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

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