3ZJF: A20P50

A20 OTU domain with irreversibly oxidised Cys103 from 270 min H2O2 soak. Determined by X-ray diffraction at 2.2 Å resolution. Released 6 Mar 2013.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
5,283
Mol. weight
86.42 kDa
Released
6 Mar 2013

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

Secondary structure: helices and β-sheets

3ZJF contains 42 α-helices and 39 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: 22 helices, 19 β-strands

ElementResiduesLengthSheet
α-helix10-134
α-helix15-2410
α-helix25-284
β-strand29-3021
α-helix36-383
β-strand39-4021
α-helix43-453
β-strand49-5022
α-helix51-522
α-helix58-6811
β-strand6913
α-helix71-799
β-strand8914
β-strand92-9432
β-strand9513
α-helix961
α-helix103-11311
α-helix121-13212
α-helix136-14813
α-helix164-17512
α-helix193-20311
β-strand207-21155
β-strand231-23335
α-helix240-2423
β-strand248-25365
β-strand256-25945
β-strand260-26342
α-helix2641
β-strand27014
β-strand272-27436
β-strand276-27947
β-strand282-28547
α-helix286-2872
β-strand28815
α-helix293-2975
α-helix299-3068
β-strand309-31466
β-strand323-32976
α-helix331-3333
α-helix337-3393
α-helix341-35414
Chain B: 20 helices, 20 β-strands
ElementResiduesLengthSheet
α-helix11-144
α-helix15-2713
β-strand29-3028
α-helix36-383
β-strand39-4028
α-helix43-453
β-strand5019
α-helix51-522
α-helix58-6811
β-strand69110
α-helix71-799
β-strand89111
β-strand92-94312
β-strand95110
α-helix961
α-helix103-11311
α-helix121-13212
α-helix136-14611
α-helix164-17411
α-helix193-20311
β-strand207-211513
β-strand231-233313
α-helix240-2423
β-strand248-253613
β-strand256-259413
β-strand260-262312
β-strand26319
β-strand270111
β-strand272-274314
β-strand276-279415
β-strand282-285415
α-helix286-2872
β-strand288113
α-helix293-2964
α-helix299-3068
β-strand309-315714
β-strand322-329814
α-helix330-3334
α-helix337-3393
α-helix341-35414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
A20P50Aprotein366HOMO SAPIENSP21580 (AlphaFold model)
A20P50Bprotein366HOMO SAPIENSP21580 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3ZJF_1 A20P50 (chains A)
MAEQVLPQALYLSNMRKAVKIRERTPEDIFKPTNGIIHHFKTMHRYTLEMFRTCQFCPQF
REIIHKALIDRNIQATLESQKKLNWCREVRKLVALKTNGDGNCLMHATSQYMWSVQDTDL
VLRKALFSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLIKMASTDTP
MARSGLQYNSLEEIHIFVLCNILRRPIIVISDKMLRSLESGSNFAPLKVGGIYLPLHWPA
QECYRYPIVLGYDSHHFVPLVTLKDSGPEIRAVPLVNRDRGRFEDLKVHFLTDPENEMKE
KLLKEYLMVIEIPVQGWDHGTTHLINAAKLDEANLPKEINLVDDYFELVQHEYKKWQENS
EQGRRE
Sequence of entity 2 (B), FASTA
>3ZJF_2 A20P50 (chains B)
MAEQVLPQALYLSNMRKAVKIRERTPEDIFKPTNGIIHHFKTMHRYTLEMFRTCQFCPQF
REIIHKALIDRNIQATLESQKKLNWCREVRKLVALKTNGDGNCLMHATSQYMWSVQDTDL
VLRKALFSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLIKMASTDTP
MARSGLQYNSLEEIHIFVLCNILRRPIIVISDKMLRSLESGSNFAPLKVGGIYLPLHWPA
QECYRYPIVLGYDSHHFVPLVTLKDSGPEIRAVPLVNRDRGRFEDLKVHFLTDPENEMKE
KLLKEYLMVIEIPVQGWDHGTTHLINAAKLDEANLPKEINLVDDYFELVQHEYKKWQENS
EQGRRE

Primary citation

Regulation of A20 and Other Otu Deubiquitinases by Reversible Oxidation. Kulathu, Y., Garcia, F.J., Mevissen, T.E.T. et al. Nat Commun (2013) 4:1569. DOI 10.1038/NCOMMS2567 · PubMed

Other PDB entries of the same protein (UniProt P21580 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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