8ROH: Structural maintenance of chromosomes protein 3

Human cohesin SMC3-HD(EQ)/RAD21-N complex - Apo conformation. Determined by X-ray diffraction at 2.6 Å resolution. Released 11 Sept 2024.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,081
Mol. weight: 67.45 kDa
Released: 11 Sept 2024

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

Secondary structure: helices and β-sheets

8ROH contains 20 α-helices and 18 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, 18 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	1
β-strand	11	1	2
β-strand	14	1	2
β-strand	18-19	2	1
α-helix	20-24	5
β-strand	27-32	6	3
α-helix	38-49	12
α-helix	51-53	3
α-helix	58-63	6
β-strand	65	1	2
β-strand	75-83	9	1
β-strand	95-103	9	1
β-strand	107-111	5	1
β-strand	114-116	3	1
α-helix	118-126	9
β-strand	138-140	3	3
α-helix	141-148	8
α-helix	152-163	12
α-helix	165-212	48
α-helix	984-988	5
α-helix	990-1023	34
α-helix	1025-1047	23
β-strand	1052-1058	7	4
β-strand	1095-1101	7	4
β-strand	1110-1111	2	4
α-helix	1117-1134	18
β-strand	1139-1143	5	3
α-helix	1151-1164	14
β-strand	1169-1173	5	3
α-helix	1178-1181	4
β-strand	1185-1191	7	3
β-strand	1196-1201	6	3
α-helix	1203-1212	10

Chain B: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	15-22	8
α-helix	24-26	3
α-helix	29-34	6
α-helix	37-45	9
α-helix	53-89	37

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Structural maintenance of chromosomes protein 3	A	protein	478	Homo sapiens	Q9UQE7 (AlphaFold model)
Double-strand-break repair protein rad21 homolog	B	protein	110	Homo sapiens	O60216 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8ROH_1 Structural maintenance of chromosomes protein 3 (chains A)
MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQ
RLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKND
VMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMK
ETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMGSGSLVPRGSGSQCNTELKKY
SHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKN
FSEVFQKLVPGGKATLVMKKGDVEGSQSQDEGEGSGESERGSGSQSSVPSVDQFTGVGIR
VSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDQIDQALDAQHRKAVSD
MIMELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG

Sequence of entity 2 (B), FASTA

>8ROH_2 Double-strand-break repair protein rad21 homolog (chains B)
MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLL
LGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEENREGSLEVLFQ

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 Q9UQE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8ROK 2.25 Å, Human cohesin SMC3-HD(EQ)/RAD21-N complex - ATP-Mg-bound conformation - Form 1
6WG4 2.31 Å, Crystal structure of human SMC1-SMC3 hinge domain heterodimer in south-open conformation
8ROI 2.45 Å, Human cohesin SMC3-HD(EQ)/RAD21-N complex - ADP-bound conformation
8ROJ 3.0 Å, Human cohesin SMC3-HD/RAD21-N complex - ADP-Mg-bound conformation
8ROL 3.11 Å, Human cohesin SMC3-HD(EQ)/RAD21-N complex - ATP-Mg-bound conformation - Form 2
6WG6 3.54 Å, Crystal structure of human SMC1-SMC3 hinge domain heterodimer in north-open conformation
8P0A 3.67 Å, Human Cohesin ATPase module
6WGE 3.9 Å, Cryo-EM structure of human Cohesin-NIPBL-DNA complex without STAG1
8PQ5 4.4 Å, Human Cohesin ATPase module with an open DNA exit gate
6WG3 5.3 Å, Cryo-EM structure of human Cohesin-NIPBL-DNA complex
7W1M 6.5 Å, Cryo-EM structure of human cohesin-CTCF-DNA complex

Browse structure collections

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