2XSZ: Ruvb-like 1

The dodecameric human RuvBL1:RuvBL2 complex with truncated domains II. Determined by X-ray diffraction at 3.0 Å resolution. Released 5 Oct 2011.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: HOMO SAPIENS
Chains: 6
Atoms: 14,664
Mol. weight: 253.3 kDa
Ligands: ATP
Released: 5 Oct 2011

Explore 2XSZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2XSZ contains 111 α-helices and 120 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: 21 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	26-29	4
α-helix	30-32	3
β-strand	40	1	1
α-helix	45	1
β-strand	46	1	1
α-helix	47	1
β-strand	49-50	2	2
β-strand	53-54	2	2
α-helix	57-71	15
β-strand	79-83	5	3
α-helix	90-100	11
β-strand	107-111	5	3
α-helix	112-115	4
α-helix	122-131	10
β-strand	134-137	4	4
β-strand	148-150	3	4
α-helix	151-157	7
α-helix	184-200	17
β-strand	204-207	4	4
β-strand	209-213	5	3
α-helix	215-217	3
β-strand	219	1	5
α-helix	220-230	11
β-strand	237-242	6	3
β-strand	246-248	3	6
α-helix	249	1
β-strand	250	1	5
β-strand	256-258	3	6
α-helix	263-266	4
β-strand	269-273	5	3
α-helix	276-278	3
α-helix	279-293	15
β-strand	297	1	7
α-helix	299-311	13
α-helix	314-319	6
α-helix	321-330	10
β-strand	336	1	7
α-helix	338-347	10
β-strand	348-349	2	8
α-helix	351-361	11

Chain B: 21 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	26-29	4
α-helix	30-32	3
β-strand	40	1	9
α-helix	45	1
β-strand	46	1	9
α-helix	47	1
β-strand	49-50	2	10
β-strand	53-54	2	10
α-helix	57-71	15
β-strand	79-83	5	11
α-helix	90-100	11
β-strand	107-111	5	11
α-helix	112-115	4
α-helix	122-131	10
β-strand	134-136	3	12
β-strand	149-150	2	12
α-helix	151-159	9
α-helix	184-200	17
β-strand	205-207	3	12
β-strand	209-213	5	11
α-helix	215-217	3
β-strand	219	1	13
α-helix	220-230	11
β-strand	237-242	6	11
β-strand	246-248	3	14
α-helix	249	1
β-strand	250	1	13
β-strand	256-258	3	14
α-helix	263-266	4
β-strand	269-273	5	11
α-helix	276-278	3
α-helix	279-292	14
β-strand	297	1	15
α-helix	299-311	13
α-helix	314-319	6
α-helix	321-330	10
β-strand	336	1	15
α-helix	338-347	10
β-strand	349	1	16
α-helix	351-361	11

Chain C: 21 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	26-29	4
α-helix	30-32	3
β-strand	40	1	17
α-helix	45	1
β-strand	46	1	17
α-helix	47	1
β-strand	49-50	2	18
β-strand	53-54	2	18
α-helix	57-71	15
β-strand	79-83	5	19
α-helix	90-100	11
β-strand	107-111	5	19
α-helix	112-115	4
α-helix	122-131	10
β-strand	134-138	5	20
β-strand	147-150	4	20
α-helix	151-158	8
α-helix	184-200	17
β-strand	203-207	5	20
β-strand	209-213	5	19
α-helix	215-217	3
β-strand	219	1	21
α-helix	220-230	11
β-strand	237-242	6	19
β-strand	246-248	3	22
α-helix	249	1
β-strand	250	1	21
β-strand	256-258	3	22
α-helix	263-266	4
β-strand	269-273	5	19
α-helix	276-278	3
α-helix	279-292	14
β-strand	297	1	23
α-helix	299-311	13
α-helix	314-319	6
α-helix	321-330	10
β-strand	336	1	23
α-helix	338-347	10
β-strand	349	1	24
α-helix	351-361	11

Chain D: 16 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	48	1	25
β-strand	54	1	25
β-strand	57-58	2	26
β-strand	61-62	2	26
α-helix	65-79	15
β-strand	87-92	6	16
α-helix	98-109	12
β-strand	115-119	5	16
α-helix	120-123	4
β-strand	125	1	27
β-strand	128	1	27
α-helix	130-140	11
β-strand	142-145	4	28
β-strand	156-158	3	28
α-helix	159-165	7
α-helix	185-201	17
β-strand	205-208	4	28
β-strand	210-214	5	16
α-helix	216-218	3
β-strand	220	1	29
α-helix	221-231	11
β-strand	238-243	6	16
β-strand	247-249	3	30
α-helix	250	1
β-strand	251	1	29
β-strand	256-258	3	30
α-helix	263-266	4
β-strand	269-274	6	16
α-helix	275-277	3
α-helix	279-293	15
β-strand	297	1	31
α-helix	299-311	13
α-helix	314-329	16
β-strand	336	1	31
α-helix	338-347	10
β-strand	349	1	3
α-helix	351-367	17

Chain E: 16 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	48	1	32
β-strand	54	1	32
β-strand	57-58	2	33
β-strand	61-62	2	33
α-helix	65-79	15
β-strand	87-92	6	24
α-helix	98-109	12
β-strand	115-119	5	24
α-helix	120-123	4
β-strand	125	1	34
β-strand	128	1	34
α-helix	130-140	11
β-strand	142-145	4	35
β-strand	156-158	3	35
α-helix	159-165	7
α-helix	185-201	17
β-strand	205-208	4	35
β-strand	210-214	5	24
α-helix	216-218	3
β-strand	220	1	36
α-helix	221-231	11
β-strand	238-243	6	24
β-strand	247-249	3	37
α-helix	250	1
β-strand	251	1	36
β-strand	256-258	3	37
α-helix	263-266	4
β-strand	269-274	6	24
α-helix	275-277	3
α-helix	279-293	15
β-strand	297	1	38
α-helix	299-311	13
α-helix	314-329	16
β-strand	336	1	38
α-helix	338-347	10
β-strand	349	1	11
α-helix	351-368	18

Chain F: 16 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	48	1	39
β-strand	54	1	39
β-strand	57-58	2	40
β-strand	61-62	2	40
α-helix	65-80	16
β-strand	87-91	5	8
α-helix	98-109	12
β-strand	115-119	5	8
α-helix	120-123	4
β-strand	125	1	41
β-strand	128	1	41
α-helix	130-140	11
β-strand	142-145	4	42
β-strand	156-158	3	42
α-helix	159-165	7
α-helix	185-201	17
β-strand	205-208	4	42
β-strand	210-214	5	8
α-helix	216-218	3
β-strand	220	1	43
α-helix	221-231	11
β-strand	238-243	6	8
β-strand	247-249	3	44
α-helix	250	1
β-strand	251	1	43
β-strand	256-258	3	44
α-helix	263-266	4
β-strand	269-273	5	8
α-helix	274-277	4
α-helix	279-293	15
β-strand	297	1	45
α-helix	299-311	13
α-helix	314-329	16
β-strand	336	1	45
α-helix	338-347	10
β-strand	348-349	2	19
α-helix	351-367	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ruvb-like 1	A, B, C	protein	367	HOMO SAPIENS	Q9Y265 (AlphaFold model)
Ruvb-like 2	D, E, F	protein	378	HOMO SAPIENS	Q9Y230 (AlphaFold model)

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

>2XSZ_1 RUVB-LIKE 1 (chains A, B, C)
MVHHHHHHLLVPRGSKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAR
EACGVIVELIKSKKMAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEI
KKTEVLMENFRRAIGLRIKEGPPGIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKT
EITDKLRGEINKVVNKYIDQGIAELVPGVLFVDEVHMLDIECFTYLHRALESSIAPIVIF
ASNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQTEGINISEE
ALNHLGEIGTKTTLRYSVQLLTPANLLAKINGKDSIEKEHVEEISELFYDAKSSAKILAD
QQDKYMK

Sequence of entity 2 (D, E, F), FASTA

>2XSZ_2 RUVB-LIKE 2 (chains D, E, F)
MDYKDDDDKENLYFQGATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQG
MVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAG
SEIFSLEMSKTEALTQAFRRSIGVRIKEGPPGVVHTVSLHEIDVINSRTQGFLALFSGDT
GEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLI
MATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTTPYSEKDTKQILRIRCEEEDVEMSED
AYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKE
YQDAFLFNELKGETMDTS

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	6

Primary citation

Structural and Functional Insights Into a Dodecameric Molecular Machine - the Ruvbl1/Ruvbl2 Complex. Gorynia, S., Bandeiras, T.M., Pinho, F.G. et al. J Struct Biol (2011) 176:279. DOI 10.1016/J.JSB.2011.09.001 · PubMed

Other PDB entries of the same protein (UniProt Q9Y265 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2C9O 2.2 Å, 3D Structure of the human RuvB-like helicase RuvBL1
8QR1 2.4 Å, Cryo-EM structure of the human Tip60 complex
9EMA 2.4 Å, RUVBL1/2 in complex with ATP and CB-6644 inhibitor
6K0R 2.5 Å, Ruvbl1-Ruvbl2 with truncated domain II in complex with phosphorylated Cordycepin
9C57 2.75 Å, Reconstituted P400 Subcomplex of the human TIP60 complex
9CAE 3.07 Å, Cryo-EM structure of the reconstituted RuvBL lobe of the human TIP60 complex (composite…
7ZI4 3.2 Å, Cryo-EM structure of the human INO80 complex bound to a WT nucleosome
8X15 3.2 Å, Structure of nucleosome-bound SRCAP-C in the apo state
8X19 3.2 Å, Structure of nucleosome-bound SRCAP-C in the ADP-BeFx-bound state
8X1C 3.2 Å, Structure of nucleosome-bound SRCAP-C in the ADP-bound state
8XVT 3.2 Å, The core subcomplex of human NuA4/TIP60 complex
9SN2 3.2 Å, Cryo-EM reconstruction of the RUVBL1-RUVBL2-CCDC103 (R2C) complex

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