3M63: Ufd2

Crystal structure of Ufd2 in complex with the ubiquitin-like (UBL) domain of Dsk2. Determined by X-ray diffraction at 2.4 Å resolution. Released 28 Apr 2010.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
8,488
Mol. weight
122.62 kDa
Released
28 Apr 2010

Explore 3M63 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3M63 contains 66 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: 64 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix-3-812
β-strand10-1121
α-helix201
β-strand21-2221
α-helix231
α-helix28-303
α-helix39-446
α-helix45-495
α-helix56-7520
α-helix80-834
α-helix84-10118
α-helix113-12210
α-helix124-1263
α-helix128-14013
α-helix144-16118
α-helix171-18616
α-helix188-1914
α-helix194-1963
α-helix202-2032
α-helix208-2103
α-helix211-2144
α-helix218-2214
α-helix228-2314
α-helix232-2365
α-helix243-27432
α-helix276-29116
α-helix294-2974
α-helix303-3053
α-helix309-32315
α-helix324-3274
α-helix334-3363
β-strand35612
α-helix361-37111
α-helix381-39212
α-helix393-3975
α-helix398-4058
α-helix407-42115
α-helix429-46032
α-helix463-48422
α-helix494-4963
α-helix501-5033
α-helix512-5176
α-helix523-5253
β-strand52712
α-helix529-54113
α-helix555-56713
α-helix575-58713
α-helix591-5922
α-helix596-5983
α-helix601-6066
α-helix608-6114
α-helix614-62411
α-helix637-65418
α-helix656-66813
α-helix670-70637
α-helix720-75435
α-helix756-7594
α-helix762-78019
α-helix782-7854
α-helix792-7954
α-helix799-81214
α-helix817-8259
α-helix832-84211
α-helix851-87828
α-helix883-8853
β-strand88613
β-strand89313
β-strand897-89934
β-strand906-90834
α-helix909-9168
β-strand92115
β-strand92815
α-helix931-9333
β-strand935-93624
α-helix938-95316
Chain B: 2 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand5-846
β-strand1616
β-strand2317
α-helix24-3512
β-strand44-4636
β-strand49-5026
β-strand5617
α-helix62-632
β-strand66-7056

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin conjugation factor E4Aprotein968Saccharomyces cerevisiaeP54860 (AlphaFold model)
Ubiquitin domain-containing protein DSK2Bprotein101Saccharomyces cerevisiaeP48510 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3M63_1 Ubiquitin conjugation factor E4 (chains A)
GSPEFRSMTAIEDILQITTDPSDTRGYSLLKSEEVPQGSTLGVDFIDTLLLYQLTENEKL
DKPFEYLNDCFRRNQQQKRITKNKPNAESLHSTFQEIDRLVIGYGVVALQIENFCMNGAF
INYITGIVSNVNSYTDFLSQIIQRAILEGTALDLLNAVFPTLLEYCNKHVSHFDLNESVI
YNNVLTIFELFVTFKPIAEIFTKIDGFFADYSCKPQDFERKTILGPILSLSPIEAAVAIR
NYGDNLLRSKQQTAMIHESLQAEHKVVIDRLFFIVDKLVRGSLNSRTDMISYFAHIANKN
HLRRADHPPFKELSSNGFMSNITLLLVRFSQPFLDISYKKIDKIDANYFNNPSLFIDLSG
ETRLNSDFKEADAFYDKNRKTADSKPNFISDCFFLTLTYLHYGLGGTLSFEEKMGSEIKA
LKEEIEKVKKIAANHDVFARFITAQLSKMEKALKTTESLRFALQGFFAHRSLQLEVFDFI
CGASTFLIRVVDPEHEFPFKQIKLPLIPDQIGVENVDNADFLRAHAPVPFKYYPEFVVEG
PVNYSLYISKYQTSPIFRNPRLGSFVEFTTMVLRCPELVSNPHLKGKLVQLLSVGAMPLT
DNSPGFMMDIFEHDELVNKNLLYALLDFYVIVEKTGSSSQFYDKFNSRYSISIILEELYY
KIPSYKNQLIWQSQNNADFFVRFVARMLNDLTFLLDEGLSNLAEVHNIQNELDNRARGAP
PTREEEDKELQTRLASASRQAKSSCGLADKSMKLFEIYSKDIPAAFVTPEIVYRLASMLN
YNLESLVGPKCGELKVKDPQSYSFNPKDLLKALTTVYINLSEQSEFISAVAKDERSFNRN
LFVRAVDILGRKTGLASPEFIEKLLNFANKAEEQRKADEEEDLEYGDVPDEFLDPLMYTI
MKDPVILPASKMNIDRSTIKAHLLSDSTDPFNRMPLKLEDVTPNEELRQKILCFKKQKKE
EAKHKASE
Sequence of entity 2 (B), FASTA
>3M63_2 Ubiquitin domain-containing protein DSK2 (chains B)
MKHHHHHHPMSDYDIPTTENLYFQGAMSLNIHIKSGQDKWEVNVAPESTVLQFKEAINKA
NGIPVANQRLIYSGKILKDDQTVESYHIQDGHSVHLVKSQP

Primary citation

The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain. Hanzelmann, P., Stingele, J., Hofmann, K. et al. J Biol Chem (2010) 285:20390-20398. DOI 10.1074/jbc.M110.112532 · PubMed

Other PDB entries of the same protein (UniProt P54860 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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