1W1W: Sc Smc1hd:Scc1-C complex, ATPgS

Sc Smc1hd:Scc1-C complex, ATPgS. Determined by X-ray diffraction at 2.9 Å resolution. Released 30 Sept 2004.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 8
Atoms: 12,360
Mol. weight: 252.6 kDa
Ligands: MG, AGS
Released: 30 Sept 2004

Explore 1W1W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1W1W contains 60 α-helices and 76 β-strands across 8 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: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	1
β-strand	18-22	5	1
β-strand	28-32	5	2
α-helix	39-49	11
α-helix	63-65	3
β-strand	91-100	10	1
β-strand	103-112	10	1
β-strand	117-121	5	1
β-strand	124-126	3	1
α-helix	128-137	10
β-strand	148-149	2	2
α-helix	156-159	4
α-helix	162-167	6
α-helix	1068-1081	14
β-strand	1096-1099	4	3
β-strand	1114-1117	4	3
α-helix	1126-1128	3
α-helix	1131-1146	16
β-strand	1153-1156	4	2
α-helix	1165-1178	14
β-strand	1180	1	4
β-strand	1183	1	4
β-strand	1184-1188	5	2
α-helix	1192-1195	4
β-strand	1200-1207	8	2
β-strand	1212-1219	8	2
α-helix	1220-1222	3

Chain B: 10 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	5
β-strand	18-22	5	5
β-strand	28-32	5	6
α-helix	39-49	11
β-strand	91-100	10	5
β-strand	103-112	10	5
β-strand	117-121	5	5
β-strand	124-126	3	5
α-helix	128-137	10
β-strand	148-149	2	6
α-helix	156-159	4
α-helix	162-173	12
α-helix	179-188	10
α-helix	1051-1081	31
β-strand	1096-1101	6	7
α-helix	1107-1109	3
β-strand	1112-1117	6	7
α-helix	1131-1146	16
β-strand	1153-1156	4	6
α-helix	1165-1178	14
β-strand	1180	1	8
β-strand	1183	1	8
β-strand	1184-1187	4	6
α-helix	1192-1195	4
β-strand	1200-1207	8	6
β-strand	1212-1219	8	6

Chain C: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	9
β-strand	18-22	5	9
β-strand	28-32	5	10
α-helix	39-49	11
β-strand	91-100	10	9
β-strand	103-112	10	9
β-strand	117-121	5	9
β-strand	124-126	3	9
α-helix	128-136	9
β-strand	148-149	2	10
α-helix	156-159	4
α-helix	162-173	12
α-helix	178-188	11
α-helix	1050-1082	33
β-strand	1096-1101	6	11
α-helix	1107-1109	3
β-strand	1112-1117	6	11
α-helix	1126-1128	3
α-helix	1131-1146	16
β-strand	1153-1156	4	10
α-helix	1165-1178	14
β-strand	1180	1	12
β-strand	1183	1	12
β-strand	1184-1188	5	10
α-helix	1192-1195	4
β-strand	1200-1207	8	10
β-strand	1212-1219	8	10
α-helix	1220-1222	3

Chain D: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	13
β-strand	18-22	5	13
β-strand	28-32	5	14
α-helix	39-49	11
β-strand	91-100	10	13
β-strand	103-112	10	13
β-strand	117-121	5	13
β-strand	124-126	3	13
α-helix	128-136	9
β-strand	148-149	2	14
α-helix	154-159	6
α-helix	162-173	12
α-helix	181-188	8
α-helix	1051-1081	31
β-strand	1096-1101	6	15
α-helix	1107-1109	3
β-strand	1112-1117	6	15
α-helix	1126-1128	3
α-helix	1131-1146	16
β-strand	1153-1156	4	14
α-helix	1165-1178	14
β-strand	1180	1	16
β-strand	1183	1	16
β-strand	1184-1188	5	14
α-helix	1192-1195	4
β-strand	1200-1207	8	14
β-strand	1212-1219	8	14

Chains E, F, G and H: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	484-495	12
β-strand	502-503	2	17
α-helix	504-509	6
α-helix	522-537	16
β-strand	540-544	5	17
β-strand	551-555	5	17
α-helix	557-559	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Structural maintenance of chromosome 1	A, B, C, D	protein	430	SACCHAROMYCES CEREVISIAE	P32908 (AlphaFold model)
Sister chromatid cohesion protein 1	E, F, G, H	protein	121	SACCHAROMYCES CEREVISIAE	Q12158 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1W1W_1 STRUCTURAL MAINTENANCE OF CHROMOSOME 1 (chains A, B, C, D)
MGRLVGLELSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSN
ILKDLIYRGVLNDENSDDYDNEGAASSNPQSAYVKAFYQKGNKLVELMRIISRNGDTSYK
IDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVEQIAAQSPVELSRMFEEVSGSIQYKK
EYEELKEKIEKLSKSATESIKNRRRIHGELKTYKSPGLEVLFQGPRGSRYDEAEGRFEVI
NNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKNPNSNVELAGG
NASLTIEDEDEPFNAGIKYHATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFV
LDEVDAALDITNVQRIAAYIRRHRNPDLQFIVISLKNTMFEKSDALVGVYRQQQENSSKI
ITLDLSNYAE

Sequence of entity 2 (E, F, G, H), FASTA

>1W1W_2 SISTER CHROMATID COHESION PROTEIN 1 (chains E, F, G, H)
MHHHHHHFPEENIIDAKTRNEQTTIQTEKVRPTPGEVASKAIVQMAKILRKELSEEKEVI
FTDVLKSQANTEPENITKREASRGFFDILSLATEGCIGLSQTEAFGNIKIDAKPALFERF
I

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	4
AGS	Phosphothiophosphoric acid-adenylate ester	C10 H16 N5 O12 P3 S	4

Primary citation

Structure and stability of cohesin's Smc1-kleisin interaction. Haering, C.H., Schoffnegger, D., Nishino, T. et al. Mol Cell (2004) 15:951-964. DOI 10.1016/j.molcel.2004.08.030 · PubMed

Other PDB entries of the same protein (UniProt P32908 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ZZ6 3.4 Å, Cryo-EM structure of S.cerevisiae cohesin-Scc2-DNA complex
7OGT 5.5 Å, Folded elbow of cohesin

Browse structure collections

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