8P0A: Human Cohesin ATPase module

Human Cohesin ATPase module. Determined by electron microscopy at 3.67 Å resolution. Released 11 Sept 2024.

Method: Electron microscopy
Resolution: 3.67 Å
Organism: Homo sapiens
Chains: 3
Atoms: 5,764
Mol. weight: 114.1 kDa
Ligands: MG, ATP
Released: 11 Sept 2024

Explore 8P0A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8P0A contains 30 α-helices and 37 β-strands across 3 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: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	1
β-strand	15	1	2
β-strand	20	1	1
β-strand	27-30	4	3
β-strand	31	1	2
α-helix	38-47	10
α-helix	68-70	3
β-strand	78-85	8	1
β-strand	92-99	8	1
β-strand	102-107	6	1
β-strand	111-112	2	1
α-helix	114-122	9
β-strand	134	1	3
α-helix	139-143	5
α-helix	148-158	11
α-helix	162-167	6
α-helix	169-173	5
α-helix	1051-1056	6
α-helix	1060-1089	30
β-strand	1095-1100	6	4
β-strand	1111-1116	6	4
α-helix	1125-1127	3
α-helix	1130-1141	12
β-strand	1152-1156	5	3
α-helix	1164-1177	14
β-strand	1183-1187	5	3
α-helix	1191-1195	5
β-strand	1199	1	3
β-strand	1202-1206	5	2
β-strand	1212-1216	5	2
α-helix	1224-1226	3

Chain B: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	5
β-strand	17	1	5
α-helix	21-24	4
β-strand	27-29	3	6
β-strand	30-32	3	7
α-helix	39-45	7
α-helix	60-63	4
α-helix	72-73	2
β-strand	76-81	6	5
β-strand	97-102	6	5
β-strand	107-111	5	5
β-strand	115-116	2	5
α-helix	118-120	3
α-helix	122-127	6
α-helix	152-161	10
α-helix	1034-1047	14
β-strand	1054-1057	4	8
β-strand	1096-1099	4	8
β-strand	1100	1	9
β-strand	1110	1	9
α-helix	1112-1114	3
α-helix	1119-1134	16
β-strand	1139-1143	5	6
α-helix	1151-1162	12
β-strand	1169-1173	5	6
α-helix	1179-1182	4
β-strand	1187-1192	6	7
β-strand	1195-1199	5	7
α-helix	1203-1211	9

Chain C: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	579	1	10
α-helix	582-584	3
α-helix	590-602	13
α-helix	603-606	4
β-strand	609-610	2	11
β-strand	622	1	10
β-strand	623-624	2	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Structural maintenance of chromosomes protein 1A	A	protein	456	Homo sapiens	Q14683 (AlphaFold model)
Structural maintenance of chromosomes protein 3	B	protein	462	Homo sapiens	Q9UQE7 (AlphaFold model)
64-kDa C-terminal product	C	protein	81	Homo sapiens	O60216 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8P0A_1 Structural maintenance of chromosomes protein 1A (chains A)
MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKT
LRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEE
LEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEE
DTQFNYHRKKNIAAERKEAKESSKHPTSLVPRGSDAQAEEEIKQEMNTLQQKLNEQQSVL
QRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESV
ATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAA
LALLFAIHSYKPAPFFVLDQIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKA
ESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ

Sequence of entity 2 (B), FASTA

>8P0A_2 Structural maintenance of chromosomes protein 3 (chains B)
MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQ
RLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKND
VMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMK
ETEGKREKINELLKYIEERLHTLEEEKEELAGSGSLVPRGSGSYSHVNKKALDQFVNFSE
QKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATL
VMKKGDVEGSQSQDEGEGSGESERGSGSQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQL
SGGQKSLVALALIFAIQKCDPAPFYLFDQIDQALDAQHRKAVSDMIMELAVHAQFITTTF
RPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG

Sequence of entity 3 (C), FASTA

>8P0A_3 64-kDa C-terminal product (chains C)
MKRTQQMLHGLQRALAKTGAESISLLELCRNTNRKQAAAKFYSFLVLKKQQAIELTQEEP
YSDIIATPGPRFHGSLEVLFQ

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

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
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

Browse structure collections

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