3CEG: Baculoviral IAP repeat-containing protein 6

Name: PDB 3CEG: Crystal structure of the UBC domain of baculoviral IAP repeat-containing protein 6
Published: 2008-04-01
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Crystal structure of the UBC domain of baculoviral IAP repeat-containing protein 6. Determined by X-ray diffraction at 2.01 Å resolution. Released 1 Apr 2008.

Method: X-ray diffraction
Resolution: 2.01 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,968
Mol. weight: 74.11 kDa
Released: 1 Apr 2008

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

Secondary structure: helices and β-sheets

3CEG contains 34 α-helices and 26 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, 13 β-strands

Element	Residues	Length	Sheet
α-helix	4496-4505	10
β-strand	4509-4512	4	1
β-strand	4515-4517	3	2
β-strand	4523-4525	3	2
α-helix	4532-4536	5
α-helix	4544-4560	17
β-strand	4569-4574	6	1
β-strand	4580-4586	7	1
β-strand	4587	1	3
α-helix	4588	1
β-strand	4594	1	3
β-strand	4597-4603	7	1
α-helix	4612-4613	2
β-strand	4614-4617	4	1
β-strand	4628	1	4
β-strand	4631	1	4
β-strand	4636	1	1
β-strand	4637	1	4
α-helix	4640-4642	3
α-helix	4649-4651	3
α-helix	4660-4666	7
α-helix	4667-4671	5
α-helix	4676-4679	4
α-helix	4683-4686	4
α-helix	4690-4706	17
α-helix	4707-4713	7
α-helix	4714-4717	4
α-helix	4724-4749	26
α-helix	4760-4782	23
α-helix	4783-4786	4

Chain B: 17 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	4496-4505	10
β-strand	4509-4512	4	5
β-strand	4515-4517	3	6
β-strand	4523-4525	3	6
α-helix	4532-4536	5
α-helix	4544-4557	14
β-strand	4569-4574	6	5
β-strand	4580-4586	7	5
β-strand	4587	1	7
α-helix	4588	1
β-strand	4594	1	7
β-strand	4597-4603	7	5
α-helix	4612-4613	2
β-strand	4614-4617	4	5
β-strand	4628	1	8
β-strand	4631	1	8
β-strand	4636	1	5
β-strand	4637	1	8
α-helix	4640-4642	3
α-helix	4660-4666	7
α-helix	4667-4671	5
α-helix	4676-4679	4
α-helix	4683-4686	4
α-helix	4690-4708	19
α-helix	4709-4713	5
α-helix	4714-4717	4
α-helix	4724-4733	10
α-helix	4735-4750	16
α-helix	4759-4782	24
α-helix	4783-4786	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Baculoviral IAP repeat-containing protein 6	A, B	protein	323	Homo sapiens	Q9NR09

Sequence of entity 1 (A, B), FASTA

>3CEG_1 Baculoviral IAP repeat-containing protein 6 (chains A, B)
ANQEKKLGEYSKKAAMKPKPLSVLKSLEEKYVAVMKKLQFDTFEMVSEDEDGKLGFKVNY
HYMSQVKNANDANSAARARRLAQEAVTLSTSLPLSSSSSVFVRCDEERLDIMKVLITGPA
DTPYANGCFEFDVYFPQDYPSSPPLVNLETTGGHSVRFNPNLYNDGKVCLSILNTWHGRP
EEKWNPQTSSFLQVLVSVQSLILVAEPYFNEPGYERSRGTPSGTQSSREYDGNIRQATVK
WAMLEQIRNPSPCFKEVIHKHFYLKRVEIMAQCEEWIADIQQYSSDKRVGRTMSHHAAAL
KRHTAQLREELLKLPCPEGLDPD

Primary citation

A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen. Sheng, Y., Hong, J.H., Doherty, R. et al. Mol Cell Proteomics (2012) 11:329-341. DOI 10.1074/mcp.O111.013706 · PubMed

Other PDB entries of the same protein (UniProt Q9NR09), best resolution first:

8E2E 1.98 Å, Cryo-EM structure of helical arch of BIRC6 (from local refinement 1)
8E2D 2.07 Å, Cryo-EM structure of BIRC6 (consensus)
8E2H 2.3 Å, Cryo-EM structure of C-terminal arm of BIRC6 (from local refinement 4)
8E2F 2.47 Å, Cryo-EM structure of N-terminal arm of BIRC6 (from local refinement 2)
8E2G 2.99 Å, Cryo-EM structure of N-terminal arm (aa68-966) of BIRC6 (from local refinement 3)
8ATO 3.0 Å, Structure of the giant inhibitor of apoptosis, BIRC6 bound to the regulator SMAC
8E2I 3.04 Å, Cryo-EM structure of BIRC6/Smac
9QH5 3.09 Å, Consensus structure of UBA6-UbDha-BIRC6 trapped ternary complex (doubly loaded)
8E2K 3.21 Å, Cryo-EM structure of BIRC6/HtrA2-S306A
8ATM 3.3 Å, Structure of the giant inhibitor of apoptosis, BIRC6 (composite map)
8ATU 3.3 Å, Cryo-EM structure of human BIRC6
9XGB 3.3 Å, UBA6-BIRC6 ubc-ubt

Browse structure collections

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