6QPQ: PDB entry 6QPQ

The structure of the cohesin head module elucidates the mechanism of ring opening. Determined by X-ray diffraction at 2.1 Å resolution. Released 5 Feb 2020.

Method: X-ray diffraction
Resolution: 2.1 Å
Organisms: Chaetomium thermophilum var. thermophilum DSM 1495, Saccharomyces cerevisiae S288C
Chains: 4
Atoms: 8,097
Mol. weight: 230.47 kDa
Released: 5 Feb 2020

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

Secondary structure: helices and β-sheets

6QPQ contains 43 α-helices and 47 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: 17 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	1
β-strand	12	1	2
β-strand	18-22	5	1
β-strand	28-32	5	3
α-helix	41-50	10
α-helix	62-65	4
β-strand	66	1	2
β-strand	117-124	8	1
β-strand	130-137	8	1
β-strand	143-147	5	1
β-strand	150-152	3	1
α-helix	154-162	9
β-strand	174-175	2	3
α-helix	177-185	9
α-helix	188-199	12
α-helix	201-204	4
α-helix	205-241	37
α-helix	244-247	4
α-helix	1066-1123	58
β-strand	1135-1140	6	4
α-helix	1147-1149	3
α-helix	1151	1
β-strand	1152-1157	6	4
α-helix	1166-1168	3
α-helix	1171-1186	16
β-strand	1193-1196	4	3
α-helix	1199-1202	4
α-helix	1205-1216	12
β-strand	1220	1	5
β-strand	1223	1	5
β-strand	1224-1228	5	3
α-helix	1232-1235	4
β-strand	1240-1247	8	3
β-strand	1252-1259	8	3
α-helix	1260-1262	3
β-strand	1264	1	6

Chain B: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	484-498	15
β-strand	501-503	3	7
α-helix	504-512	9
α-helix	516-518	3
β-strand	520	1	6
α-helix	521-536	16
β-strand	540-543	4	7
β-strand	552-555	4	7
α-helix	557-560	4

Chain C: 16 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	8
β-strand	12	1	9
β-strand	18-22	5	8
β-strand	28-32	5	10
α-helix	41-50	10
α-helix	62-65	4
β-strand	66	1	9
β-strand	117-124	8	8
β-strand	130-137	8	8
β-strand	143-147	5	8
β-strand	150-152	3	8
α-helix	154-163	10
β-strand	174-175	2	10
α-helix	177-185	9
α-helix	188-199	12
α-helix	201-204	4
α-helix	205-239	35
α-helix	1066-1123	58
β-strand	1135-1140	6	11
α-helix	1147-1149	3
β-strand	1152-1157	6	11
β-strand	1164-1165	2	11
α-helix	1166-1168	3
α-helix	1171-1186	16
β-strand	1193-1196	4	10
α-helix	1199-1202	4
α-helix	1205-1218	14
β-strand	1220	1	12
β-strand	1223	1	12
β-strand	1224-1228	5	10
α-helix	1232-1235	4
β-strand	1240-1247	8	10
β-strand	1252-1259	8	10
α-helix	1260-1262	3
β-strand	1264	1	13
α-helix	1265	1

Chain D: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	484-496	13
β-strand	502-503	2	14
α-helix	504-512	9
α-helix	516-518	3
β-strand	520	1	13
α-helix	521-536	16
β-strand	540-543	4	14
β-strand	552-555	4	14
α-helix	557-560	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein	A, C	protein	453	Chaetomium thermophilum var. thermophilum DSM 1495	G0SGH3 (AlphaFold model)
Sister chromatid cohesion protein 1	B, D	protein	566	Saccharomyces cerevisiae S288C	Q12158 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6QPQ_1 Structural maintenance of chromosomes protein,Structural maintenance of chromosomes protein (chains A, C)
MGKLIRLELFNFKSYKGHHTLLFGDSYFTSIIGPNGSGKSNSMDAISFVLGIKSSHLRSS
NLRDLIYRGRVMKTSKIQDDGTTAPATNGDVNGYENGDAGDDEDTSQRTSRNDPKTAWVM
AVYEDDAGELHRWKRTITANGTSEYRINDRVVNAQQYNEALEKENILIKARNFLVFQGDV
EAIASQSPQDLTRLIEQISGSLEYKEEYERLEEEVRQATEEQAYKLQRRRAANSEIKQYM
EQSPGLEVLFMDRLDHVRKQLEQTEQEFEASKAKLRQARESFQAVKQKRLELFNKAFTHI
QEQITHVYKELTRSEAYPLGGQAYLDIEEDTDTPFLSGVKYHAMPPLKRFRDMEHLSGGE
KTMAALALLFAIHSYQPSPFFVLDEVDAALDNANVEKIKKYIREHAGPGMQFIVISLKPA
LFQASESLIGVYRDQEANTSRTLTLDLRKYRHH

Sequence of entity 2 (B, D), FASTA

>6QPQ_2 Sister chromatid cohesion protein 1 (chains B, D)
MVTENPQRLTVLRLATNKGPLAQIWLASNMSNIPRGSVIQTHIAESAKEIAKASGCDDES
GDNEYITLRTSGELLQGIVRVYSKQATFLLTDIKDTLTKISMLFKTSQKMTSTVNRLNTV
TRVHQLMLEDAVTEREVLVTPGLEFLDDTTIPVGLMAQENSMERKVQGAAPWDTSLEVGR
RFSPDEDFEHNNLSSMNLDFDIEEGPITSKSWEEGTRQSSRNFDTHENYIQDDDFPLDDA
GTIGWDLGITEKNDQNNDDDDNSVEQGRRLGESIMSEEPTDFGFDLDIEKEAPAGNIDTI
TDAMTESQPKQTGTRRNSKLLNTKSIQIDEETENSESIASSNTYKEERSNNLLTPQPTNF
TTKRLWSEITESMSYLPDPILKNFLSYESLKKRKIHNGREGSIEEPELNVSLNLTDDVIS
NAGTNDNSFNELTDNMSDFVPIDAGLNEAPFPEENIIDAKTRNEQTTIQTEKVRPTPGEV
ASKAIVQMAKILRKELSEEKEVIFTDVLKSQANTEPENITKREASRGFFDILSLATEGCI
GLSQTEAFGNIKIDAKPALFERFINA

Primary citation

The structure of the cohesin ATPase elucidates the mechanism of SMC-kleisin ring opening. Muir, K.W., Li, Y., Weis, F. et al. Nat Struct Mol Biol (2020) 27:233-239. DOI 10.1038/s41594-020-0379-7 · PubMed

Other PDB entries of the same protein (UniProt G0SGH3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6QPW 3.3 Å, Structural basis of cohesin ring opening

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