1C4Z: Ubiquitin-protein ligase E3A

Name: PDB 1C4Z: Structure of an E6AP-UBCH7 complex: insights into the ubiquitination pathway
Published: 1999-11-17
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Structure of an E6AP-UBCH7 complex: insights into the ubiquitination pathway. Determined by X-ray diffraction at 2.6 Å resolution. Released 17 Nov 1999.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,040
Mol. weight: 142.51 kDa
Released: 17 Nov 1999

Explore 1C4Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1C4Z contains 61 α-helices and 51 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: 20 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	502-504	3	1
α-helix	509-522	14
α-helix	525-529	5
α-helix	531-532	2
β-strand	534-536	3	1
α-helix	546-559	14
α-helix	562-564	3
β-strand	567-570	4	2
β-strand	575-578	4	2
α-helix	586-601	16
α-helix	612-618	7
α-helix	621-623	3
α-helix	625-631	7
α-helix	633-644	12
α-helix	649-652	4
β-strand	656	1	3
β-strand	658-661	4	4
β-strand	669-672	4	4
β-strand	681	1	3
α-helix	687-699	13
α-helix	704-718	15
α-helix	730-737	8
β-strand	739	1	5
β-strand	752-754	3	6
α-helix	762-772	11
α-helix	776-786	11
β-strand	792	1	5
α-helix	797-800	4
β-strand	803-809	7	6
α-helix	813-815	3
β-strand	816-818	3	6
α-helix	819-821	3
β-strand	823-828	6	6
α-helix	832-845	14

Chain B: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	502-504	3	7
α-helix	509-522	14
α-helix	525-529	5
β-strand	534-536	3	7
α-helix	546-559	14
α-helix	562-564	3
β-strand	567-570	4	8
β-strand	575-578	4	8
α-helix	586-601	16
α-helix	613-618	6
α-helix	621-623	3
α-helix	625-627	3
α-helix	628-631	4
α-helix	633-644	12
β-strand	656	1	9
β-strand	658-662	5	10
β-strand	668-672	5	10
β-strand	681	1	9
α-helix	687-699	13
α-helix	704-718	15
α-helix	730-737	8
β-strand	739	1	11
β-strand	752-754	3	12
α-helix	762-772	11
α-helix	776-786	11
β-strand	792	1	11
α-helix	797-800	4
β-strand	803-809	7	12
α-helix	813-815	3
β-strand	816-818	3	12
α-helix	819-821	3
β-strand	823-828	6	12
α-helix	832-845	14

Chain C: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	499	1	13
β-strand	502-504	3	14
α-helix	509-522	14
α-helix	525-529	5
β-strand	531	1	13
β-strand	534-536	3	14
α-helix	546-559	14
α-helix	562-564	3
β-strand	567-570	4	15
β-strand	575-578	4	15
α-helix	586-601	16
α-helix	612-618	7
α-helix	621-623	3
α-helix	625-631	7
α-helix	633-644	12
β-strand	656	1	16
β-strand	658-662	5	17
β-strand	668-672	5	17
β-strand	681	1	16
α-helix	687-699	13
α-helix	704-718	15
α-helix	730-737	8
β-strand	739	1	18
β-strand	752-754	3	19
α-helix	762-772	11
α-helix	776-786	11
β-strand	792	1	18
α-helix	797-800	4
β-strand	803-809	7	19
α-helix	813-815	3
β-strand	816-818	3	19
α-helix	819-821	3
β-strand	823-828	6	19
α-helix	832-845	14

Chain D: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	7-11	5
β-strand	23-25	3	20
β-strand	34-39	6	20
β-strand	51-56	6	20
β-strand	67-70	4	20
β-strand	79	1	21
β-strand	84	1	20
β-strand	85	1	21
α-helix	101-113	13
α-helix	123-130	8
α-helix	137-144	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-protein ligase E3A	A, B, C	protein	358	Homo sapiens	Q05086 (AlphaFold model)
Ubiquitin conjugating enzyme E2	D	protein	154	Homo sapiens	P68036 (AlphaFold model)

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

>1C4Z_1 UBIQUITIN-PROTEIN LIGASE E3A (chains A, B, C)
QLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQL
VVEEIFNPDIGMFTYDESTKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVV
YRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLK
ENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIEL
LICGSRNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPV
GGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML

Sequence of entity 2 (D), FASTA

>1C4Z_2 UBIQUITIN CONJUGATING ENZYME E2 (chains D)
MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAE
YPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHP
LRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD

Primary citation

Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Huang, L., Kinnucan, E., Wang, G. et al. Science (1999) 286:1321-1326. DOI 10.1126/science.286.5443.1321 · PubMed

Other PDB entries of the same protein (UniProt Q05086 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6TGK 1.3 Å, Domain swapped E6AP C-lobe dimer
6SJV 2.03 Å, Structure of HPV18 E6 oncoprotein in complex with mutant E6AP LxxLL motif
4XR8 2.25 Å, Crystal structure of the HPV16 E6/E6AP/p53 ternary complex at 2.25 A resolution
7QPB 2.34 Å, Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid…
4GIZ 2.55 Å, Crystal structure of full-length human papillomavirus oncoprotein E6 in complex with…
9L3L 2.59 Å, Crystal structure of the C lobe of E6AP in complex with K48-linked diUb
8JRN 2.6 Å, Structure of E6AP-E6 complex in Att1 state
1D5F 2.8 Å, Structure of E6AP: insights into ubiquitination pathway
6SLM 2.8 Å, Crystal structure of full-length HPV31 E6 oncoprotein in complex with LXXLL peptide of…
8JRO 3.01 Å, Structure of E6AP-E6 complex in Att2 state
7Q41 3.01 Å, Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with…
9U4A 3.3 Å, Structure of UBE3A T485E tetramer

Browse structure collections

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