3ZJD: A20 OTU domain in reduced, active state

A20 OTU domain in reduced, active state at 1.87 A resolution. Determined by X-ray diffraction at 1.87 Å resolution. Released 6 Mar 2013.

Method: X-ray diffraction
Resolution: 1.87 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 5,508
Mol. weight: 86.51 kDa
Released: 6 Mar 2013

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

Secondary structure: helices and β-sheets

3ZJD contains 41 α-helices and 40 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, 20 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
α-helix	15-27	13
β-strand	29-30	2	1
α-helix	36-38	3
β-strand	39-40	2	1
α-helix	43-45	3
β-strand	50	1	2
α-helix	51-52	2
α-helix	58-68	11
β-strand	69	1	3
α-helix	71-79	9
β-strand	89	1	4
β-strand	92-94	3	5
β-strand	95	1	3
α-helix	96	1
α-helix	103-113	11
α-helix	121-132	12
α-helix	136-147	12
α-helix	164-174	11
α-helix	189-191	3
α-helix	193-203	11
β-strand	207-211	5	6
β-strand	231-233	3	6
α-helix	240-242	3
β-strand	248-253	6	6
β-strand	256-259	4	6
β-strand	260-262	3	5
β-strand	263	1	2
α-helix	264	1
β-strand	270	1	4
β-strand	272-274	3	7
β-strand	276-279	4	8
β-strand	282-285	4	8
α-helix	286-287	2
β-strand	288	1	6
α-helix	293-297	5
α-helix	299-306	8
β-strand	309-315	7	7
β-strand	322-329	8	7
α-helix	331-333	3
α-helix	337-339	3
α-helix	341-354	14

Chain B: 19 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
α-helix	15-28	14
β-strand	29-30	2	9
α-helix	37-38	2
β-strand	39-40	2	9
α-helix	43-45	3
β-strand	50	1	10
α-helix	51-52	2
α-helix	58-68	11
β-strand	69	1	11
α-helix	71-79	9
β-strand	89	1	12
β-strand	92-94	3	13
β-strand	95	1	11
α-helix	96	1
α-helix	103-113	11
α-helix	121-131	11
α-helix	136-147	12
α-helix	167-174	8
α-helix	193-203	11
β-strand	207-211	5	14
β-strand	231-233	3	14
α-helix	240-242	3
β-strand	248-253	6	14
β-strand	256-259	4	14
β-strand	260-262	3	13
β-strand	263	1	10
β-strand	270	1	12
β-strand	272-274	3	15
β-strand	276-279	4	16
β-strand	282-285	4	16
α-helix	286-287	2
β-strand	288	1	14
α-helix	293-296	4
α-helix	299-306	8
β-strand	309-315	7	15
β-strand	322-329	8	15
α-helix	330-333	4
α-helix	341-355	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
A20P50	A, B	protein	366	HOMO SAPIENS	P21580 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3ZJD_1 A20P50 (chains A, 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:

3VUX 1.7 Å, Crystal structure of A20 ZF7 in complex with linear ubiquitin, form II
3ZJE 1.84 Å, A20 OTU domain in reversibly oxidised (SOH) state
3ZJG 1.92 Å, A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.
3VUW 1.95 Å, Crystal structure of A20 ZF7 in complex with linear ubiquitin, form I
3VUY 1.98 Å, Crystal structure of A20 ZF7 in complex with linear tetraubiquitin
3ZJF 2.2 Å, A20 OTU domain with irreversibly oxidised Cys103 from 270 min H2O2 soak.
3DKB 2.5 Å, Crystal Structure of A20, 2.5 angstrom
3OJ3 2.5 Å, Crystal structure of the A20 ZnF4 and ubiquitin complex
5V3P 2.5 Å, Human A20 OTU domain (I325N) with acetamidylated C103
5LRX 2.85 Å, Structure of A20 OTU domain bound to ubiquitin
5V3B 3.0 Å, Human A20 OTU domain (WT) with acetamidylated C103
2VFJ 3.2 Å, Structure of the A20 Ovarian Tumour (OTU) domain

Browse structure collections

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