6WG6: Structural maintenance of chromosomes protein

Crystal structure of human SMC1-SMC3 hinge domain heterodimer in north-open conformation. Determined by X-ray diffraction at 3.54 Å resolution. Released 20 May 2020.

Method: X-ray diffraction
Resolution: 3.54 Å
Organism: Homo sapiens
Chains: 14
Atoms: 20,038
Mol. weight: 342.79 kDa
Released: 20 May 2020

Explore 6WG6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6WG6 contains 153 α-helices and 118 β-strands across 12 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: 11 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	496-510	15
β-strand	515-518	4	1
α-helix	520-522	3
β-strand	524-525	2	2
α-helix	531-538	8
α-helix	539-543	5
β-strand	545-547	3	1
α-helix	550-562	13
β-strand	568-572	5	1
α-helix	583-586	4
β-strand	592-593	2	3
α-helix	595-597	3
β-strand	598-599	2	2
α-helix	603-605	3
α-helix	606-613	8
β-strand	617-619	3	3
α-helix	622-630	9
β-strand	638-640	3	3
β-strand	645-646	2	3
β-strand	652-653	2	3
α-helix	659-675	17

Chain B: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	471-500	30
α-helix	502-519	18
α-helix	525-528	4
β-strand	531-534	4	4
α-helix	536-538	3
β-strand	539-540	2	5
α-helix	543-545	3
α-helix	546-553	8
α-helix	554-558	5
α-helix	559	1
β-strand	560-562	3	4
α-helix	565-578	14
β-strand	586-588	3	4
α-helix	589-591	3
β-strand	605-607	3	1
α-helix	609-611	3
β-strand	613-614	2	5
α-helix	616-618	3
α-helix	619-625	7
β-strand	629-632	4	1
α-helix	635-645	11
β-strand	648-650	3	1
β-strand	656-657	2	1
β-strand	663-665	3	1
α-helix	674-700	27

Chain C: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	496-510	15
β-strand	515-518	4	6
α-helix	519-522	4
β-strand	523-525	3	7
α-helix	531-538	8
α-helix	539-543	5
α-helix	544	1
β-strand	545-547	3	6
α-helix	550-562	13
β-strand	568-571	4	6
α-helix	580-582	3
α-helix	583-585	3
β-strand	592-593	2	8
β-strand	598-600	3	7
α-helix	603-605	3
α-helix	606-612	7
β-strand	617-619	3	8
α-helix	622-630	9
β-strand	638-640	3	8
β-strand	645-646	2	8
β-strand	652-653	2	8
α-helix	659-675	17

Chain D: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	469-500	32
α-helix	502-520	19
α-helix	525-528	4
β-strand	531-534	4	9
β-strand	539-540	2	10
α-helix	543-545	3
α-helix	546-553	8
α-helix	554-558	5
β-strand	560-562	3	9
α-helix	565-578	14
β-strand	586-588	3	9
α-helix	589-591	3
β-strand	605-607	3	6
α-helix	609-611	3
β-strand	613-614	2	10
α-helix	616-618	3
α-helix	619-625	7
β-strand	630-632	3	6
α-helix	635-644	10
β-strand	649-651	3	6
β-strand	656-657	2	6
β-strand	663-665	3	6
α-helix	674-700	27

Chain E: 10 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	495-510	16
β-strand	515-518	4	11
α-helix	519-522	4
β-strand	523-525	3	12
α-helix	531-538	8
α-helix	539-543	5
α-helix	544	1
β-strand	545-547	3	11
α-helix	550-563	14
β-strand	568-571	4	11
α-helix	583-587	5
β-strand	592-593	2	13
β-strand	598-600	3	12
α-helix	606-613	8
β-strand	617-618	2	13
α-helix	622-631	10
β-strand	638-639	2	13
β-strand	645-646	2	13
β-strand	652-653	2	13
α-helix	656-670	15

Chain F: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	471-500	30
α-helix	502-520	19
α-helix	525-530	6
β-strand	531-534	4	14
α-helix	536-538	3
β-strand	539-540	2	15
α-helix	543-545	3
α-helix	546-553	8
α-helix	554-558	5
β-strand	559-562	4	14
α-helix	565-577	13
β-strand	585-588	4	14
α-helix	589-591	3
β-strand	605-607	3	11
α-helix	608-611	4
β-strand	613-614	2	15
α-helix	616-618	3
α-helix	619-625	7
β-strand	629-632	4	11
α-helix	635-645	11
β-strand	648-651	4	11
β-strand	656-657	2	11
β-strand	663-665	3	11
α-helix	674-700	27

Chain G: 10 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	495-510	16
β-strand	515-518	4	16
α-helix	519-522	4
β-strand	523-525	3	17
α-helix	531-538	8
α-helix	539-542	4
α-helix	544	1
β-strand	545-547	3	16
α-helix	550-563	14
β-strand	568-571	4	16
α-helix	583-586	4
β-strand	592-593	2	18
β-strand	598-600	3	17
α-helix	606-613	8
β-strand	617-618	2	18
α-helix	622-630	9
β-strand	638-639	2	18
β-strand	645-646	2	18
β-strand	652-653	2	18
α-helix	659-669	11

Chain H: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	471-500	30
α-helix	502-520	19
α-helix	525-529	5
β-strand	531-534	4	19
α-helix	536-538	3
β-strand	539-540	2	20
α-helix	543-545	3
α-helix	546-553	8
α-helix	554-558	5
β-strand	560-562	3	19
α-helix	565-578	14
β-strand	586-588	3	19
α-helix	589-591	3
β-strand	605-607	3	16
α-helix	608-611	4
β-strand	613-614	2	20
α-helix	616-618	3
α-helix	619-626	8
β-strand	629-632	4	16
α-helix	635-645	11
β-strand	648-650	3	16
β-strand	656-657	2	16
β-strand	663-665	3	16
α-helix	674-700	27

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Structural maintenance of chromosomes protein	A, C, E, G, I, K	protein	233	Homo sapiens	Q14683 (AlphaFold model)
Structural maintenance of chromosomes protein 3	B, D, F, H, J, L	protein	256	Homo sapiens	Q9UQE7 (AlphaFold model)
poly(dT)	M, N	DNA	10	Homo sapiens

Sequence of entity 1 (A, C, E, G, I, K), FASTA

>6WG6_1 Structural maintenance of chromosomes protein (chains A, C, E, G, I, K)
GPEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKK
YQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELK
GAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKS
GVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQ

Sequence of entity 2 (B, D, F, H, J, L), FASTA

>6WG6_2 Structural maintenance of chromosomes protein 3 (chains B, D, F, H, J, L)
GPLGSGRPQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLD
HFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFN
KMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSME
VSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLN
ENLRRNIERINNEIDQ

Sequence of entity 3 (M, N), FASTA

>6WG6_3 poly(dT) (chains M, N)
TTTTTTTTTT

Primary citation

Cryo-EM structure of the human cohesin-NIPBL-DNA complex. Shi, Z., Gao, H., Bai, X.C. et al. Science (2020) 368:1454-1459. DOI 10.1126/science.abb0981 · PubMed

Other PDB entries of the same protein (UniProt Q14683 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8ROE 1.36 Å, Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ADP-bound conformation
8ROD 1.5 Å, Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - Open/closed P-loop conformation
8ROF 1.65 Å, Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ADP-Mg-bound conformation
8RO9 1.77 Å, Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - Open/closed P-loop conformation
8ROC 1.85 Å, Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - Apo closed P-loop conformation
8RO8 1.9 Å, Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - Apo closed P-loop conformation
8ROG 1.94 Å, Human cohesin SMC1A-HD(shortCC-EQ)/RAD21-C complex - ATPgS-Mg-bound conformation
8RO7 2.09 Å, Human cohesin SMC1A-HD(longCC)/RAD21-C complex - Open/closed P-loop conformation
8RO6 2.2 Å, Human cohesin SMC1A-HD(longCC)/RAD21-C complex - Apo closed P-loop conformation
6WG4 2.31 Å, Crystal structure of human SMC1-SMC3 hinge domain heterodimer in south-open conformation
8ROA 2.44 Å, Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - ADP-bound conformation
8ROB 2.5 Å, Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - ATPgS-Mg-bound conformation

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