4A0C: CAND1-CUL4B-RBX1 complex

Structure of the CAND1-CUL4B-RBX1 complex. Determined by X-ray diffraction at 3.8 Å resolution. Released 30 Nov 2011.

Method: X-ray diffraction
Resolution: 3.8 Å
Organisms: HOMO SAPIENS, MUS MUSCULUS
Chains: 6
Atoms: 30,804
Mol. weight: 475.43 kDa
Ligands: ZN
Released: 30 Nov 2011

Explore 4A0C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4A0C contains 245 α-helices and 48 β-strands across 6 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: 76 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	8-14	7
α-helix	20-33	14
α-helix	46-56	11
α-helix	62-76	15
α-helix	81-96	16
α-helix	100-115	16
α-helix	127-142	16
α-helix	148-162	15
α-helix	170-172	3
α-helix	173-180	8
α-helix	181-183	3
α-helix	189-205	17
α-helix	208-224	17
α-helix	228-231	4
α-helix	233-244	12
α-helix	248-250	3
α-helix	257-264	8
α-helix	269-283	15
α-helix	293-299	7
α-helix	347-361	15
α-helix	368-372	5
α-helix	373-375	3
α-helix	377-380	4
α-helix	388-404	17
α-helix	424-442	19
α-helix	448-464	17
α-helix	473-475	3
α-helix	477-485	9
α-helix	491-506	16
α-helix	514-516	3
α-helix	517-528	12
α-helix	533-550	18
α-helix	562-576	15
α-helix	583-599	17
α-helix	607-617	11
α-helix	625-636	12
α-helix	645-657	13
α-helix	658-660	3
α-helix	665-680	16
α-helix	687-694	8
α-helix	706-722	17
α-helix	726-729	4
α-helix	734-742	9
α-helix	749-760	12
α-helix	772-780	9
α-helix	781-783	3
α-helix	797-807	11
α-helix	813-825	13
α-helix	832-845	14
α-helix	858-861	4
α-helix	864-866	3
α-helix	870-885	16
α-helix	888-901	14
α-helix	903-905	3
α-helix	906-917	12
α-helix	922-925	4
α-helix	926-928	3
α-helix	929-938	10
α-helix	946-961	16
α-helix	963-974	12
α-helix	981-988	8
α-helix	1001-1012	12
α-helix	1021-1036	16
α-helix	1038-1040	3
α-helix	1045-1054	10
β-strand	1063-1065	3	1
β-strand	1074-1076	3	1
α-helix	1077-1079	3
α-helix	1080-1095	16
α-helix	1097-1099	3
α-helix	1102-1111	10
α-helix	1117-1133	17
α-helix	1135-1141	7
α-helix	1142-1145	4
α-helix	1147-1154	8
α-helix	1156-1158	3
α-helix	1163-1184	22
α-helix	1193-1202	10

Chain B: 80 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	5-13	9
α-helix	20-34	15
α-helix	44-55	12
α-helix	62-70	9
α-helix	72-77	6
α-helix	81-93	13
α-helix	102-113	12
α-helix	114-116	3
α-helix	125-142	18
α-helix	151-162	12
α-helix	167-169	3
α-helix	173-180	8
α-helix	181-183	3
α-helix	189-205	17
α-helix	210-223	14
α-helix	228-244	17
α-helix	247-250	4
α-helix	251-254	4
α-helix	257-264	8
α-helix	269-285	17
α-helix	293-301	9
α-helix	347-363	17
α-helix	365-367	3
α-helix	368-374	7
α-helix	376-380	5
α-helix	382-384	3
α-helix	389-405	17
α-helix	424-442	19
α-helix	448-464	17
α-helix	473-485	13
α-helix	491-506	16
α-helix	514-528	15
α-helix	533-550	18
α-helix	562-564	3
α-helix	565-576	12
α-helix	583-599	17
α-helix	608-619	12
α-helix	625-635	11
α-helix	645-658	14
α-helix	664-673	10
α-helix	675-678	4
α-helix	682-684	3
α-helix	690-693	4
α-helix	694-696	3
α-helix	706-722	17
α-helix	727-729	3
α-helix	733-742	10
α-helix	749-763	15
α-helix	772-780	9
α-helix	781-783	3
α-helix	795-807	13
α-helix	815-821	7
α-helix	832-845	14
α-helix	857-864	8
α-helix	870-886	17
α-helix	888-901	14
α-helix	903-905	3
α-helix	906-919	14
α-helix	922-925	4
α-helix	926-928	3
α-helix	929-937	9
α-helix	945-959	15
α-helix	963-970	8
α-helix	973-976	4
α-helix	980-989	10
α-helix	1001-1010	10
α-helix	1022-1036	15
α-helix	1045-1055	11
α-helix	1058-1059	2
β-strand	1063	1	2
β-strand	1066	1	3
β-strand	1073	1	3
β-strand	1076	1	2
α-helix	1077-1079	3
α-helix	1080-1091	12
α-helix	1102-1110	9
α-helix	1117-1127	11
α-helix	1135-1140	6
α-helix	1146-1154	9
α-helix	1156-1158	3
α-helix	1163-1173	11
α-helix	1178-1185	8
α-helix	1193-1204	12
α-helix	1206-1209	4

Chain C: 39 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	224-227	4
α-helix	237-243	7
α-helix	257-262	6
α-helix	265-268	4
α-helix	272-274	3
α-helix	282-306	25
α-helix	308-310	3
α-helix	324-332	9
α-helix	333-337	5
α-helix	343-359	17
α-helix	365-377	13
α-helix	381-385	5
α-helix	386-407	22
α-helix	410-430	21
α-helix	437-448	12
α-helix	453-460	8
α-helix	462-465	4
α-helix	470-482	13
α-helix	486-506	21
α-helix	511-513	3
α-helix	515-532	18
α-helix	541-551	11
α-helix	558-570	13
β-strand	572	1	4
α-helix	585-594	10
α-helix	601-616	16
β-strand	620	1	4
α-helix	623-634	12
α-helix	643-653	11
α-helix	659-665	7
β-strand	676-683	8	5
α-helix	684-686	3
α-helix	699-712	14
β-strand	719-723	5	5
β-strand	729-731	3	5
β-strand	734-735	2	6
β-strand	740-741	2	6
β-strand	743-746	4	5
α-helix	747-750	4
β-strand	762-763	2	7
α-helix	764-771	8
α-helix	775-781	7
α-helix	783-787	5
β-strand	793-795	3	7
β-strand	807-810	4	7
β-strand	821-822	2	5
α-helix	830-831	2
α-helix	832-860	29
β-strand	863-865	3	8
α-helix	870-876	7
α-helix	883-893	11
α-helix	894-896	3
β-strand	900-901	2	8
β-strand	908-910	3	8

Chain D: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	22	1	6
β-strand	26-35	10	5
α-helix	54-57	4
α-helix	65-67	3
β-strand	70-72	3	9
β-strand	78-80	3	9
α-helix	81-85	5
α-helix	86-88	3
β-strand	105-106	2	9

Chain E: 43 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	212-216	5
α-helix	224-227	4
α-helix	240-244	5
α-helix	254-268	15
α-helix	272-275	4
α-helix	282-306	25
α-helix	308-310	3
α-helix	311-315	5
α-helix	316-317	2
α-helix	322-323	2
α-helix	324-335	12
α-helix	342-357	16
α-helix	365-377	13
α-helix	381-385	5
α-helix	386-403	18
α-helix	410-430	21
α-helix	434-436	3
α-helix	437-444	8
α-helix	445-449	5
α-helix	453-459	7
α-helix	461-466	6
α-helix	470-480	11
α-helix	486-505	20
α-helix	509-511	3
α-helix	516-532	17
α-helix	538-552	15
α-helix	558-569	12
α-helix	584-594	11
α-helix	601-616	16
α-helix	625-631	7
α-helix	640-643	4
α-helix	647-669	23
β-strand	676-677	2	10
β-strand	680-683	4	11
α-helix	690-692	3
α-helix	701-704	4
α-helix	706-712	7
β-strand	714	1	12
β-strand	717	1	12
β-strand	719-734	16	11
β-strand	742-746	5	11
α-helix	747-754	8
α-helix	755-757	3
β-strand	762-763	2	13
α-helix	764-771	8
α-helix	775-781	7
β-strand	793-795	3	13
β-strand	807-810	4	13
β-strand	821-822	2	11
α-helix	826-828	3
α-helix	832-860	29
β-strand	863-865	3	14
α-helix	870-876	7
α-helix	883-894	12
β-strand	900-901	2	14
β-strand	908-910	3	14

Chain F: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	22-24	3	11
β-strand	26-27	2	10
β-strand	28-35	8	11
α-helix	38-40	3
β-strand	70	1	15
β-strand	71-72	2	16
β-strand	80	1	15
α-helix	81-90	10
β-strand	93	1	17
β-strand	100	1	17
α-helix	101	1
β-strand	105-106	2	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cullin-associated NEDD8-dissociated protein 1	A, B	protein	1253	HOMO SAPIENS	Q86VP6 (AlphaFold model)
Cullin-4B	C, E	protein	741	HOMO SAPIENS	Q13620 (AlphaFold model)
E3 ubiquitin-protein ligase RBX1	D, F	protein	98	MUS MUSCULUS	P62878 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4A0C_1 CULLIN-ASSOCIATED NEDD8-DISSOCIATED PROTEIN 1 (chains A, B)
MASWSHPQFEKVDENLYFQGGGRMASASYHISNLLEKMTSSDKDFRFMATNDLMTELQKD
SIKLDDDSERKVVKMILKLLEDKNGEVQNLAVKCLGPLVSKVKEYQVETIVDTLCTNMLS
DKEQLRDISSIGLKTVIGELPPASSGSALAANVCKKITGRLTSAIAKQEDVSVQLEALDI
MADMLSRQGGLLVNFHPSILTCLLPQLTSPRLAVRKRTIIALGHLVMSCGNIVFVDLIEH
LLSELSKNDSMSTTRTYIQCIAAISRQAGHRIGEYLEKIIPLVVKFCNVDDDELREYCIQ
AFESFVRRCPKEVYPHVSTIINICLKYLTYDPNYNYDDEDEDENAMDADGGDDDDQGSDD
EYSDDDDMSWKVRRAAAKCLDAVVSTRHEMLPEFYKTVSPALISRFKEREENVKADVFHA
YLSLLKQTRPVQSWLCDPDAMEQGETPLTMLQSQVPNIVKALHKQMKEKSVKTRQCCFNM
LTELVNVLPGALTQHIPVLVPGIIFSLNDKSSSSNLKIDALSCLYVILCNHSPQVFHPHV
QALVPPVVACVGDPFYKITSEALLVTQQLVKVIRPLDQPSSFDATPYIKDLFTCTIKRLK
AADIDQEVKERAISCMGQIICNLGDNLGSDLPNTLQIFLERLKNEITRLTTVKALTLIAG
SPLKIDLRPVLGEGVPILASFLRKNQRALKLGTLSALDILIKNYSDSLTAAMIDAVLDEL
PPLISESDMHVSQMAISFLTTLAKVYPSSLSKISGSILNELIGLVRSPLLQGGALSAMLD
FFQALVVTGTNNLGYMDLLRMLTGPVYSQSTALTHKQSYYSIAKCVAALTRACPKEGPAV
VGQFIQDVKNSRSTDSIRLLALLSLGEVGHHIDLSGQLELKSVILEAFSSPSEEVKSAAS
YALGSISVGNLPEYLPFVLQEITSQPKRQYLLLHSLKEIISSASVVGLKPYVENIWALLL
KHCECAEEGTRNVVVECLGKLTLIDPETLLPRLKGYLISGSSYARSSVVTAVKFTISDHP
QPIDPLLKNCIGDFLKTLEDPDLNVRRVALVTFNSAAHNKPSLIRDLLDTVLPHLYNETK
VRKELIREVEMGPFKHTVDDGLDIRKAAFECMYTLLDSCLDRLDIFEFLNHVEDGLKDHY
DIKMLTFLMLVRLSTLCPSAVLQRLDRLVEPLRATCTTKVKANSVKQEFEKQDELKRSAM
RAVAALLTIPEAEKSPLMSEFQSQISSNPELAAIFESIQKDSSSTNLESMDTS

Sequence of entity 2 (C, E), FASTA

>4A0C_2 CULLIN-4B (chains C, E)
MHHHHHHVDENLYFQGGGRGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTS
IKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRC
WQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQNKTIDGILL
LIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPE
YLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAILQKGLNNLLDENRIQD
LSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDI
CFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMI
IFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDM
ELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFY
LGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATG
IEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETV
EEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIES
LIDRDYMERDKENPNQYNYIA

Sequence of entity 3 (D, F), FASTA

>4A0C_3 E3 UBIQUITIN-PROTEIN LIGASE RBX1 (chains D, F)
MGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTV
AWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	6

Primary citation

The Molecular Basis of Crl4(Ddb2/Csa) Ubiquitin Ligase Architecture, Targeting, and Activation. Scrima, A., Fischer, E.S., Iwai, S. et al. Cell (2011) 147:1024. DOI 10.1016/J.CELL.2011.10.035 · PubMed

Other PDB entries of the same protein (UniProt Q86VP6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7Z8R 2.7 Å, CAND1-CUL1-RBX1
7Z8V 2.7 Å, CAND1-SCF-SKP2 (SKP1deldel) CAND1 engaged SCF rocked
8OR3 2.9 Å, CAND1-CUL1-RBX1-SKP1-SKP2-DCNL1
7Z8T 3.0 Å, CAND1-SCF-SKP2 CAND1 engaged SCF rocked
1U6G 3.1 Å, Crystal Structure of The Cand1-Cul1-Roc1 Complex
7ZBZ 3.1 Å, CAND1 delhairpin-SCF-SKP2 CAND1 partly engaged SCF partly rocked
8OR0 3.1 Å, CAND1-CUL1-RBX1-SKP1-SKP2-CKS1-CDK2
8OR2 3.2 Å, CAND1-CUL1-RBX1-DCNL1
8CDK 3.32 Å, CAND1 b-hairpin++-SCF-SKP2 CAND1 partly engaged SCF partly rocked
8CDJ 3.4 Å, CAND1 b-hairpin++-SCF-SKP2 CAND1 rolling SCF engaged
7ZBW 3.5 Å, CAND1-SCF-SKP2 CAND1 rolling-2 SCF engaged
8H3Q 3.76 Å, Cryo-EM Structure of the CAND1-Cul3-Rbx1 complex

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