6ZQH: Yeast Uba1

Yeast Uba1 in complex with ubiquitin. Determined by X-ray diffraction at 2.03 Å resolution. Released 4 Nov 2020.

Method: X-ray diffraction
Resolution: 2.03 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 18,867
Mol. weight: 246.8 kDa
Released: 4 Nov 2020

Explore 6ZQH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6ZQH contains 138 α-helices and 120 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: 67 helices, 52 β-strands

Element	Residues	Length	Sheet
α-helix	16-26	11
α-helix	28-34	7
β-strand	38-42	5	1
α-helix	46-58	13
β-strand	62-66	5	1
β-strand	70	1	2
α-helix	71	1
α-helix	73-77	5
α-helix	84-86	3
β-strand	90	1	2
α-helix	91-100	10
β-strand	108-110	3	1
α-helix	117-122	6
β-strand	125-128	4	1
α-helix	134-147	14
β-strand	150-157	8	1
β-strand	158	1	3
β-strand	160-166	7	1
β-strand	171-173	3	4
β-strand	175	1	5
α-helix	179-182	4
β-strand	183-185	3	6
β-strand	186-189	4	7
β-strand	194-197	4	7
β-strand	210-214	5	6
β-strand	217	1	8
α-helix	220-223	4
β-strand	228-229	2	6
β-strand	231-232	2	7
β-strand	237-239	3	7
α-helix	244-246	3
β-strand	251	1	8
β-strand	254-258	5	6
α-helix	259-261	3
β-strand	262-264	3	4
α-helix	269-274	6
β-strand	278	1	1
α-helix	279-280	2
α-helix	283-285	3
α-helix	286-305	20
α-helix	309-312	4
α-helix	316-332	17
α-helix	334-337	4
α-helix	341-343	3
α-helix	345-354	10
β-strand	358	1	3
α-helix	360-379	20
β-strand	381	1	5
α-helix	383-385	3
β-strand	388-392	5	1
α-helix	394-396	3
α-helix	398-399	2
α-helix	418-424	7
α-helix	426-433	8
β-strand	436-440	5	9
α-helix	444-456	13
β-strand	465-469	5	9
α-helix	472	1
β-strand	473	1	10
α-helix	474	1
α-helix	476-478	3
α-helix	487-489	3
β-strand	493	1	10
α-helix	494-505	12
α-helix	507-509	3
β-strand	513-516	4	9
α-helix	522-524	3
α-helix	530-535	6
β-strand	538-541	4	9
α-helix	546-559	14
β-strand	563-569	7	9
β-strand	572-578	7	9
β-strand	583	1	11
α-helix	586-588	3
α-helix	592-598	7
α-helix	599-603	5
α-helix	609-621	13
α-helix	622-626	5
α-helix	627-636	10
α-helix	640-646	7
α-helix	651-663	13
α-helix	669-681	13
α-helix	682-686	5
α-helix	687-694	8
β-strand	700	1	12
β-strand	706	1	12
α-helix	725-742	18
α-helix	752-754	3
α-helix	755-763	9
α-helix	768-770	3
α-helix	796-804	9
α-helix	806-807	2
α-helix	808-810	3
α-helix	830-844	15
α-helix	847-849	3
α-helix	852-859	8
α-helix	862-864	3
α-helix	867-885	19
α-helix	891-893	3
β-strand	896-900	5	9
β-strand	905-909	5	9
β-strand	910	1	13
α-helix	911-912	2
β-strand	913	1	11
α-helix	914-915	2
β-strand	916-919	4	14
β-strand	922-925	4	14
β-strand	930-934	5	15
β-strand	938	1	16
α-helix	939-949	11
β-strand	953-959	7	17
β-strand	962-966	5	17
α-helix	971-977	7
β-strand	981	1	16
α-helix	982-990	9
β-strand	1000-1003	4	15
β-strand	1004-1008	5	17
β-strand	1014-1015	2	17
β-strand	1019-1023	5	15

Chains B and D: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	13
β-strand	12-16	5	13
β-strand	22	1	18
α-helix	23-34	12
α-helix	38-40	3
β-strand	42-45	4	13
β-strand	48-49	2	13
β-strand	55	1	18
α-helix	57-59	3
β-strand	66-70	5	13
β-strand	75	1	9

Chain C: 65 helices, 52 β-strands

Element	Residues	Length	Sheet
α-helix	16-26	11
α-helix	28-34	7
β-strand	38-42	5	19
α-helix	46-58	13
β-strand	62-66	5	19
β-strand	70	1	20
α-helix	71	1
α-helix	73-77	5
α-helix	84-86	3
β-strand	90	1	20
α-helix	91-100	10
β-strand	108-110	3	19
α-helix	117-122	6
β-strand	125-128	4	19
α-helix	134-147	14
β-strand	150-157	8	19
β-strand	158	1	21
β-strand	160-166	7	19
β-strand	171-173	3	22
β-strand	175	1	23
α-helix	179-182	4
β-strand	183-185	3	24
β-strand	186-189	4	25
β-strand	194-197	4	25
β-strand	210-214	5	24
β-strand	217	1	26
α-helix	220-223	4
β-strand	228-229	2	24
β-strand	231-232	2	25
β-strand	237-239	3	25
α-helix	244-246	3
β-strand	251	1	26
β-strand	254-258	5	24
β-strand	262-264	3	22
α-helix	269-274	6
β-strand	278	1	19
α-helix	283-285	3
α-helix	286-305	20
α-helix	309-312	4
α-helix	316-332	17
α-helix	334-337	4
α-helix	341-343	3
α-helix	345-353	9
β-strand	358	1	21
α-helix	360-379	20
β-strand	381	1	23
α-helix	383-385	3
β-strand	388-392	5	19
α-helix	394-396	3
α-helix	398-399	2
α-helix	418-424	7
α-helix	426-433	8
β-strand	436-440	5	27
α-helix	444-456	13
β-strand	465-469	5	27
α-helix	472	1
β-strand	473	1	28
α-helix	474	1
α-helix	476-478	3
α-helix	487-489	3
β-strand	493	1	28
α-helix	494-505	12
α-helix	507-509	3
β-strand	513-516	4	27
α-helix	522-524	3
α-helix	530-535	6
β-strand	538-541	4	27
α-helix	546-559	14
β-strand	563-569	7	27
β-strand	572-578	7	27
β-strand	583	1	29
α-helix	586-588	3
α-helix	592-598	7
α-helix	599-603	5
α-helix	609-621	13
α-helix	622-626	5
α-helix	627-636	10
α-helix	640-646	7
α-helix	651-663	13
α-helix	669-681	13
α-helix	682-686	5
α-helix	687-694	8
β-strand	700	1	30
β-strand	706	1	30
α-helix	725-742	18
α-helix	751-753	3
α-helix	755-763	9
α-helix	765-770	6
α-helix	795-804	10
α-helix	805-807	3
α-helix	830-844	15
α-helix	847-849	3
α-helix	852-859	8
α-helix	862-864	3
α-helix	867-885	19
α-helix	891-893	3
β-strand	896-900	5	27
β-strand	905-909	5	27
β-strand	910	1	31
α-helix	911-912	2
β-strand	913	1	29
α-helix	914-915	2
β-strand	916-919	4	32
β-strand	922-925	4	32
β-strand	931-934	4	33
β-strand	938	1	34
α-helix	939-949	11
β-strand	953-959	7	35
β-strand	962-966	5	35
α-helix	971-977	7
β-strand	981	1	34
α-helix	982-990	9
α-helix	993-995	3
β-strand	1000-1003	4	33
β-strand	1004-1008	5	35
β-strand	1014-1015	2	35
β-strand	1020-1023	4	33

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-activating enzyme E1 1	A, C	protein	1024	Saccharomyces cerevisiae	P22515 (AlphaFold model)
Ubiquitin-40S ribosomal protein S31	B, D	protein	76	Saccharomyces cerevisiae	P05759 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6ZQH_1 Ubiquitin-activating enzyme E1 1 (chains A, C)
MSSNNSGLSAAGEIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGV
KSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAYVPVNVLDSLDDVTQL
SQFQVVVATDTVSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDLGDEFTVLDPTGEE
PRTGMVSDIEPDGTVTMLDDNRHGLEDGNFVRFSEVEGLDKLNDGTLFKVEVLGPFAFRI
GSVKEYGEYKKGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAAQLHLGFQALH
QFAVRHNGELPRTMNDEDANELIKLVTDLSVQQPEVLGEGVDVNEDLIKELSYQARGDIP
GVVAFFGGLVAQEVLKACSGKFTPLKQFMYFDSLESLPDPKNFPRNEKTTQPVNSRYDNQ
IAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSGSDGYIVVTDNDSIEKSNLN
RQFLFRPKDVGKNKSEVAAEAVCAMNPDLKGKINAKIDKVGPETEEIFNDSFWESLDFVT
NALDNVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRDPPEKSIPLC
TLRSFPNKIDHTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLKQSGDVKGVLESISD
SLSSKPHNFEDCIKWARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEF
DIYNNDHFHFVVAGASLRAYNYGIKSDDSNSKPNVDEYKSVIDHMIIPEFTPNANLKIQV
NDDDPDPNANAANGSDEIDQLVSSLPDPSTLAGFKLEPVDFEKDDDTNHHIEFITACSNC
RAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGFVN
LALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKLSDLIEHFEKDEGLEITMLSYG
VSLLYASFFPPKKLKERLNLPITQLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFI
TIHL

Sequence of entity 2 (B, D), FASTA

>6ZQH_2 Ubiquitin-40S ribosomal protein S31 (chains B, D)
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Primary citation

Development of ADPribosyl Ubiquitin Analogues to Study Enzymes Involved in Legionella Infection. Kim, R.Q., Misra, M., Gonzalez, A. et al. Chemistry (2021) 27:2506-2512. DOI 10.1002/chem.202004590 · PubMed

Other PDB entries of the same protein (UniProt P22515 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7ZH9 1.72 Å, Uba1 in complex with ATP
6NYA 2.06 Å, Crystal Structure of ubiquitin E1 (Uba1) in complex with Ubc3 (Cdc34) and ubiquitin
5TR4 2.2 Å, Structure of Ubiquitin activating enzyme (Uba1) in complex with ubiquitin and TAK-243
5L6H 2.3 Å, Uba1 in complex with Ub-ABPA3 covalent adduct
6ZHT 2.3 Å, Uba1-Ubc13 disulfide mediated complex
6ZHS 2.35 Å, Uba1 bound to two E2 (Ubc13) molecules
4NNJ 2.4 Å, Crystal structure of Uba1 in complex with ubiquitin-AMP and thioesterified ubiquitin
5L6J 2.68 Å, Uba1 in complex with Ub-MLN7243 covalent adduct
3CMM 2.7 Å, Crystal Structure of the Uba1-Ubiquitin Complex
5L6I 2.76 Å, Uba1 in complex with Ub-MLN4924 covalent adduct
6ZHU 3.18 Å, Yeast Uba1 in complex with Ubc3 and ATP
7K5J 3.42 Å, Structure of an E1-E2-ubiquitin thioester mimetic

Browse structure collections

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