3HTK: Mms21 and Smc5 complex

Crystal structure of Mms21 and Smc5 complex. Determined by X-ray diffraction at 2.31 Å resolution. Released 20 Oct 2009.

Method: X-ray diffraction
Resolution: 2.31 Å
Organism: Saccharomyces cerevisiae
Chains: 3
Atoms: 3,222
Mol. weight: 46.2 kDa
Ligands: ZN
Released: 20 Oct 2009

Explore 3HTK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HTK contains 16 α-helices and 9 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	307-360	54

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	743-808	66

Chain C: 14 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	16-18	3
α-helix	19-24	6
α-helix	27-29	3
α-helix	31-51	21
α-helix	60-99	40
α-helix	102-104	3
α-helix	108-114	7
α-helix	122-127	6
α-helix	142-155	14
β-strand	159	1	1
β-strand	179	1	1
β-strand	183	1	2
β-strand	190	1	2
β-strand	194-197	4	3
β-strand	203-205	3	3
α-helix	206-212	7
β-strand	219-220	2	4
α-helix	221	1
α-helix	223-225	3
β-strand	229-230	2	4
α-helix	232-234	3
β-strand	235-237	3	3
α-helix	239-256	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Structural maintenance of chromosomes protein 5	A	protein	60	Saccharomyces cerevisiae	Q08204 (AlphaFold model)
Structural maintenance of chromosomes protein 5	B	protein	73	Saccharomyces cerevisiae	Q08204 (AlphaFold model)
E3 SUMO-protein ligase MMS21	C	protein	267	Saccharomyces cerevisiae	P38632 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3HTK_1 Structural maintenance of chromosomes protein 5 (chains A)
KPFANTKKTLENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNEYYR

Sequence of entity 2 (B), FASTA

>3HTK_2 Structural maintenance of chromosomes protein 5 (chains B)
DVSQKIKDIDDQIQQLLLKQRHLLSKMASSMKSLKNCQKELISTQILQFEAQNMDVSMND
VIGFFNEREADLK

Sequence of entity 3 (C), FASTA

>3HTK_3 E3 SUMO-protein ligase MMS21 (chains C)
MALNDNPIPKSVPLHPKSGKYFHNLHARDLSNIYQQCYKQIDETINQLVDSTSPSTIGIE
EQVADITSTYKLLSTYESESNSFDEHIKDLKKNFKQSSDACPQIDLSTWDKYRTGELTAP
KLSELYLNMPTPEPATMVNNTDTLKILKVLPYIWNDPTCVIPDLQNPADEDDLQIEGGKI
ELTCPITCKPYEAPLISRKCNHVFDRDGIQNYLQGYTTRDCPQAACSQVVSMRDFVRDPI
MELRCKIAKMKESQEQDKRSSQAIDVL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex. Duan, X., Sarangi, P., Liu, X. et al. Mol Cell (2009) 35:657-668. DOI 10.1016/j.molcel.2009.06.032 · PubMed

Other PDB entries of the same protein (UniProt Q08204 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8HQS 3.2 Å, Cryo-EM structure of 8-subunit Smc5/6 head region
7P47 3.31 Å, Structure of the E3 ligase Smc5/Nse2 in complex with Ubc9-SUMO thioester mimetic
7TVE 3.8 Å, ATP and DNA bound SMC5/6 core complex
8T8F 4.8 Å, Smc5/6 8mer
8WJN 5.58 Å, Cryo-EM structure of 6-subunit Smc5/6 head region
7YQH 5.6 Å, Cryo-EM structure of 8-subunit Smc5/6
8I4V 5.97 Å, Cryo-EM structure of 5-subunit Smc5/6 arm region
8I4W 6.01 Å, Cryo-EM structure of 5-subunit Smc5/6 head region
8I21 6.02 Å, Cryo-EM structure of 6-subunit Smc5/6 arm region
8WJO 6.04 Å, Cryo-EM structure of 8-subunit Smc5/6 arm region
8WJL 6.15 Å, Cryo-EM structure of 6-subunit Smc5/6 hinge region
7YLM 6.17 Å, Cryo-EM structure of 8-subunit Smc5/6 hinge region

Browse structure collections

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