8RO9: Structural maintenance of chromosomes protein 1A

Human cohesin SMC1A-HD(longCC-EQ)/RAD21-C complex - Open/closed P-loop conformation. Determined by X-ray diffraction at 1.77 Å resolution. Released 11 Sept 2024.

Method: X-ray diffraction
Resolution: 1.77 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,877
Mol. weight: 121.58 kDa
Ligands: B3P
Released: 11 Sept 2024

Explore 8RO9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8RO9 contains 35 α-helices and 38 β-strands across 4 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: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	1
β-strand	15-21	7	1
β-strand	27-31	5	2
α-helix	38-48	11
α-helix	53-55	3
α-helix	61-64	4
β-strand	65	1	1
α-helix	68-70	3
β-strand	77-86	10	1
β-strand	89-99	11	1
β-strand	102-107	6	1
β-strand	110-112	3	1
α-helix	114-123	10
β-strand	134-135	2	2
α-helix	139-144	6
α-helix	148-158	11
α-helix	161-164	4
α-helix	165-181	17
α-helix	1046-1089	44
β-strand	1095-1100	6	3
α-helix	1106-1108	3
β-strand	1111-1116	6	3
β-strand	1123-1124	2	3
α-helix	1125-1127	3
α-helix	1130-1145	16
β-strand	1152-1156	5	2
α-helix	1158-1161	4
α-helix	1167-1178	12
β-strand	1183-1187	5	2
α-helix	1191-1194	4
β-strand	1199-1206	8	2
β-strand	1212-1219	8	2

Chain B: 3 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	579-580	2	4
α-helix	581-585	5
α-helix	590-605	16
β-strand	609-613	5	4
β-strand	620-624	5	4
α-helix	632-635	4

Chain C: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-12	10	5
β-strand	15-21	7	5
β-strand	27-31	5	6
α-helix	38-48	11
α-helix	53-55	3
α-helix	61-64	4
β-strand	65	1	5
α-helix	68-70	3
β-strand	78-85	8	5
β-strand	92-99	8	5
β-strand	102-107	6	5
β-strand	110-112	3	5
α-helix	114-123	10
β-strand	134-135	2	6
α-helix	139-143	5
α-helix	148-159	12
α-helix	1064-1089	26
β-strand	1095-1100	6	7
α-helix	1106-1108	3
β-strand	1111-1116	6	7
β-strand	1123-1124	2	7
α-helix	1125-1127	3
α-helix	1130-1145	16
β-strand	1152-1156	5	6
α-helix	1167-1178	12
β-strand	1183-1187	5	6
α-helix	1191-1194	4
β-strand	1199-1206	8	6
β-strand	1212-1219	8	6

Chain D: 3 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	579-580	2	8
α-helix	581-584	4
α-helix	590-605	16
β-strand	609-613	5	8
β-strand	620-624	5	8
α-helix	632-635	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Structural maintenance of chromosomes protein 1A	A, C	protein	456	Homo sapiens	Q14683 (AlphaFold model)
64-kDa C-terminal product	B, D	protein	81	Homo sapiens	O60216 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>8RO9_1 Structural maintenance of chromosomes protein 1A (chains A, C)
MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKT
LRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEE
LEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEE
DTQFNYHRKKNIAAERKEAKESSKHPTSLVPRGSDAQAEEEIKQEMNTLQQKLNEQQSVL
QRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESV
ATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAA
LALLFAIHSYKPAPFFVLDQIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKA
ESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ

Sequence of entity 2 (B, D), FASTA

>8RO9_2 64-kDa C-terminal product (chains B, D)
MKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEP
YSDIIATPGPRFHGSLEVLFQ

Ligands and cofactors

ID	Name	Formula	Copies
B3P	2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-pr…	C11 H26 N2 O6	1

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:

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

Browse structure collections

About this viewer

MolViewer shows 8RO9 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.