8RO7: Structural maintenance of chromosomes protein 1A

Human cohesin SMC1A-HD(longCC)/RAD21-C complex - Open/closed P-loop conformation. Determined by X-ray diffraction at 2.09 Å resolution. Released 11 Sept 2024.

Method
X-ray diffraction
Resolution
2.09 Å
Organism
Homo sapiens
Chains
2
Atoms
3,188
Mol. weight
60.65 kDa
Released
11 Sept 2024

Explore 8RO7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8RO7 contains 16 α-helices and 21 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: 13 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand3-12101
β-strand15-2171
β-strand27-3152
α-helix38-4811
α-helix53-553
α-helix61-644
β-strand6511
α-helix68-703
β-strand78-8581
β-strand92-9981
β-strand102-10761
β-strand110-11231
α-helix114-12310
β-strand134-13522
α-helix139-1446
α-helix148-15912
α-helix165-1684
α-helix1064-108825
β-strand1095-110063
β-strand1111-111663
β-strand1123-112423
α-helix1131-114515
β-strand1152-115652
α-helix1158-11614
α-helix1167-117812
β-strand1183-118752
α-helix1191-11944
β-strand1199-120682
β-strand1212-121982
Chain B: 3 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand579-58024
α-helix581-5844
α-helix590-60516
β-strand609-61354
β-strand620-62454
β-strand62515
β-strand62815
α-helix632-6354

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Structural maintenance of chromosomes protein 1A (SMC1A)Aprotein456Homo sapiensQ14683 (AlphaFold model)
64-kDa C-terminal productBprotein81Homo sapiensO60216 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8RO7_1 Structural maintenance of chromosomes protein 1A (SMC1A) (chains A)
MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKT
LRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEE
LEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEE
DTQFNYHRKKNIAAERKEAKESSKHPTSLVPRGSDAQAEEEIKQEMNTLQQKLNEQQSVL
QRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESV
ATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAA
LALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKA
ESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ
Sequence of entity 2 (B), FASTA
>8RO7_2 64-kDa C-terminal product (chains B)
MKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEP
YSDIIATPGPRFHGSLEVLFQ

Primary citation

The cohesin ATPase cycle is mediated by specific conformational dynamics and interface plasticity of SMC1A and SMC3 ATPase domains. Vitoria Gomes, M., Landwerlin, P., Diebold-Durand, M.L. et al. Cell Rep (2024) 43:114656-114656. DOI 10.1016/j.celrep.2024.114656 · PubMed

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

Browse structure collections

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