6WG4: Structural maintenance of chromosomes protein

Crystal structure of human SMC1-SMC3 hinge domain heterodimer in south-open conformation. Determined by X-ray diffraction at 2.31 Å resolution. Released 20 May 2020.

Method: X-ray diffraction
Resolution: 2.31 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,974
Mol. weight: 42.92 kDa
Released: 20 May 2020

Explore 6WG4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6WG4 contains 28 α-helices and 19 β-strands across 2 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: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	500-510	11
β-strand	515-518	4	1
α-helix	519-522	4
β-strand	523-525	3	2
α-helix	528-530	3
α-helix	531-538	8
α-helix	539-543	5
β-strand	545-547	3	1
α-helix	550-562	13
α-helix	565-567	3
β-strand	570-572	3	1
α-helix	579-581	3
α-helix	583-587	5
β-strand	591-593	3	3
α-helix	595-597	3
β-strand	598-600	3	2
α-helix	603-605	3
α-helix	606-613	8
β-strand	617-619	3	3
α-helix	622-630	9
β-strand	638-639	2	3
β-strand	645-646	2	3
β-strand	652-654	3	3
α-helix	656-663	8
α-helix	665-668	4

Chain B: 13 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	503-522	20
α-helix	526-531	6
β-strand	532-535	4	3
α-helix	536-539	4
β-strand	541	1	4
α-helix	544-546	3
α-helix	547-554	8
α-helix	555-559	5
α-helix	560	1
β-strand	561-563	3	3
α-helix	566-578	13
β-strand	585-589	5	3
α-helix	600-602	3
β-strand	606-608	3	5
α-helix	609-612	4
β-strand	614	1	4
α-helix	617-619	3
α-helix	620-627	8
β-strand	630-633	4	5
α-helix	636-645	10
β-strand	649-652	4	5
β-strand	657-658	2	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Structural maintenance of chromosomes protein	A	protein	179	Homo sapiens	Q14683 (AlphaFold model)
Structural maintenance of chromosomes protein 3	B	protein	201	Homo sapiens	Q9UQE7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6WG4_1 Structural maintenance of chromosomes protein (chains A)
GPRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDC
IQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNA
LVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLK

Sequence of entity 2 (B), FASTA

>6WG4_2 Structural maintenance of chromosomes protein 3 (chains B)
GPLGSGRPKQQLLRAATGKAILNGIDSINKVLDHFRRKGINQHVQNGYHGIVMNNFECEP
AFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVRDTAYPETN
DAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGAL
TGGYYDTRKSRLELQKDVRKA

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
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
6WG6 3.54 Å, Crystal structure of human SMC1-SMC3 hinge domain heterodimer in north-open conformation

Browse structure collections

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