3T6P: Baculoviral IAP repeat-containing protein 2

IAP antagonist-induced conformational change in cIAP1 promotes E3 ligase activation via dimerization. Determined by X-ray diffraction at 1.9 Å resolution. Released 2 Nov 2011.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,845
Mol. weight: 39.47 kDa
Ligands: ZN
Released: 2 Nov 2011

Explore 3T6P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3T6P contains 26 α-helices and 10 β-strands across 1 chain. 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: 26 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	269-275	7
α-helix	276-278	3
α-helix	287-292	6
β-strand	295-297	3	1
β-strand	304-306	3	1
β-strand	312-313	2	1
α-helix	322-329	8
α-helix	334-340	7
α-helix	342-351	10
α-helix	355-361	7
α-helix	389-391	3
α-helix	394-401	8
α-helix	406-420	15
α-helix	427-450	24
α-helix	452-455	4
α-helix	456-463	8
α-helix	465-471	7
α-helix	476-484	9
α-helix	490-497	8
α-helix	502-516	15
α-helix	518-531	14
α-helix	533-536	4
α-helix	537-541	5
α-helix	553-555	3
α-helix	558-566	9
β-strand	570	1	2
β-strand	578	1	2
α-helix	579	1
β-strand	581-584	4	1
β-strand	589-591	3	1
α-helix	596-598	3
β-strand	601	1	3
α-helix	607	1
β-strand	608	1	3
α-helix	609	1
β-strand	611-614	4	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Baculoviral IAP repeat-containing protein 2	A	protein	345	Homo sapiens	Q13490 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3T6P_1 Baculoviral IAP repeat-containing protein 2 (chains A)
GSMQTHAARMRTFMYWPSSVPVQPEQLASAGFYYVGRNDDVKCFSCDGGLRCWESGDDPW
VEHAKWFPRCEFLIRMKGQEFVDEIQGRYPHLLEQLLSTPPIIHYGPGESSSEDAVMMNT
PVVKSALEMGFNRDLVKQTVQSKILTTGENYKTVNDIVSALLNAEDEKREEEKEKQAEEM
ASDDLSLIRKNRMALFQQLTCVLPILDNLLKANVINKQEHDIIKQKTQIPLQARELIDTI
LVKGNAAANIFKNSLKEIDSTLYKNLFVDKNMKYIPTEDVSGLSLEEQLRRLQEERTCKV
CMDKEVSVVFIPCGHLVVCQECAPSLRKCPICRGIIKGTVRTFLS

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	3

Primary citation

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination. Dueber, E.C., Schoeffler, A.J., Lingel, A. et al. Science (2011) 334:376-380. DOI 10.1126/science.1207862 · PubMed

Other PDB entries of the same protein (UniProt Q13490 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4HY4 1.25 Å, Crystal structure of cIAP1 BIR3 bound to T3170284
7QGJ 1.3 Å, Apo structure of BIR2 Domain of BIRC2
3D9T 1.5 Å, CIAP1-BIR3 in complex with N-terminal peptide from Caspase-9 (ATPFQE)
8DSF 1.5 Å, Structure of cIAP1 with BCCov
4KMN 1.52 Å, Structure of cIAP1-BIR3 and inhibitor
4LGE 1.55 Å, Crystal structure of clAP1 BIR3 bound to T3261256
6HPR 1.7 Å, Crystal structure of cIAP1 RING domain bound to UbcH5B-Ub and a non-covalent Ub
7TRL 1.74 Å, Crystal structure of human BIRC2 BIR3 domain in complex with histone H3
4HY5 1.75 Å, Crystal structure of cIAP1 BIR3 bound to T3256336
3UW4 1.79 Å, Crystal structure of cIAP1 BIR3 bound to GDC0152
4MU7 1.79 Å, Crystal structure of cIAP1 BIR3 bound to T3450325
5M6N 1.8 Å, Small Molecule inhibitors of IAP

Browse structure collections

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