4L1M: First RCC1-like domain of HERC2

Structure of the first RCC1-like domain of HERC2. Determined by X-ray diffraction at 2.6 Å resolution. Released 3 Jul 2013.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 3
Atoms: 7,981
Mol. weight: 127.24 kDa
Released: 3 Jul 2013

Explore 4L1M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4L1M contains 32 α-helices and 84 β-strands across 3 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.

Chains A and C: 11 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	425-429	5	1
β-strand	443-444	2	1
α-helix	446-449	4
β-strand	453-458	6	2
β-strand	462-467	6	2
β-strand	472-476	5	2
β-strand	485-486	2	2
β-strand	495-499	5	3
β-strand	506-511	6	3
β-strand	516-520	5	3
α-helix	523-525	3
β-strand	535-540	6	3
α-helix	542-544	3
α-helix	549-551	3
β-strand	553-558	6	4
β-strand	562-567	6	4
β-strand	572-576	5	4
α-helix	579-581	3
β-strand	591-596	6	4
α-helix	598-600	3
β-strand	605-610	6	5
β-strand	616-621	6	5
β-strand	626-630	5	5
α-helix	633-635	3
β-strand	645-650	6	5
α-helix	652-654	3
β-strand	659-665	7	6
β-strand	668-673	6	6
β-strand	678-682	5	6
α-helix	685-687	3
β-strand	697-702	6	6
α-helix	704-706	3
β-strand	711-716	6	7
β-strand	720-725	6	7
β-strand	730-735	6	7
β-strand	748-754	7	7
α-helix	755	1
β-strand	763-768	6	1
β-strand	772-777	6	1

Chain B: 10 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	425-429	5	8
β-strand	443-444	2	8
α-helix	446-449	4
β-strand	453-458	6	9
β-strand	462-467	6	9
β-strand	472-476	5	9
β-strand	485-486	2	9
β-strand	495-499	5	10
β-strand	506-511	6	10
β-strand	516-520	5	10
α-helix	523-525	3
β-strand	535-540	6	10
α-helix	542-544	3
β-strand	553-558	6	11
β-strand	562-567	6	11
β-strand	572-576	5	11
α-helix	579-581	3
β-strand	591-596	6	11
α-helix	598-600	3
β-strand	605-610	6	12
β-strand	616-621	6	12
β-strand	626-630	5	12
α-helix	633-635	3
β-strand	645-650	6	12
α-helix	652-654	3
β-strand	659-665	7	13
β-strand	668-673	6	13
β-strand	678-682	5	13
α-helix	685-687	3
β-strand	697-702	6	13
α-helix	704-706	3
β-strand	711-716	6	14
β-strand	720-725	6	14
β-strand	730-735	6	14
β-strand	748-754	7	14
α-helix	755	1
β-strand	763-768	6	8
β-strand	772-777	6	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase HERC2	A, B, C	protein	392	Homo sapiens	O95714

Sequence of entity 1 (A, B, C), FASTA

>4L1M_1 E3 ubiquitin-protein ligase HERC2 (chains A, B, C)
MHHHHHHSSGRENLYFQGSHKGSLQEVIGWGLIGWKYYANVIGPIQCEGLANLGVTQIAC
AEKRFLILSRNGRVYTQAYNSDTLAPQLVQGLASRNIVKIAAHSDGHHYLALAATGEVYS
WGCGDGGRLGHGDTVPLEEPKVISAFSGKQAGKHVVHIACGSTYSAAITAEGELYTWGRG
NYGRLGHGSSEDEAIPMLVAGLKGLKVIDVACGSGDAQTLAVTENGQVWSWGDGDYGKLG
RGGSDGCKTPKLIEKLQDLDVVKVRCGSQFSIALTKDGQVYSWGKGDNQRLGHGTEEHVR
YPKLLEGLQGKKVIDVAAGSTHCLALTEDSEVHSWGSNDQCQHFDTLRVTKPEPAALPGL
DTKHIVGIACGPAQSFAWSSCSEWSIGLRVPF

Primary citation

Structure of the first RCC1-like domain of HERC2. Tempel, W., Khan, M.B., Dong, A. et al. To be published.

Other PDB entries of the same protein (UniProt O95714), best resolution first:

9L93 1.73 Å, Crystal structure of NCOA4 in complex with HERC2
3KCI 1.8 Å, The third RLD domain of HERC2
9L8Y 1.92 Å, Crystal structure of HERC2
7Q42 1.95 Å, Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with…
7RGW 1.99 Å, Crystal structure of HERC2 DOC domain
6WW3 2.1 Å, Crystal structure of HERC2 ZZ domain in complex with SUMO1 tail
7Q45 2.1 Å, Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with…
7Q44 2.2 Å, Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with…
6WW4 2.25 Å, Crystal structure of HERC2 ZZ domain in complex with histone H3 tail
7Q40 2.35 Å, Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2
7Q43 2.4 Å, Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with…
7Q46 2.46 Å, Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with…

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