2AYN: Ubiquitin carboxyl-terminal hydrolase 14

Name: PDB 2AYN: Structure of USP14, a proteasome-associated deubiquitinating enzyme
Published: 2005-10-18
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: hydrolase

Structure of USP14, a proteasome-associated deubiquitinating enzyme. Determined by X-ray diffraction at 3.2 Å resolution. Released 18 Oct 2005.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 3
Atoms: 8,163
Mol. weight: 138.63 kDa
Released: 18 Oct 2005

Explore 2AYN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2AYN contains 52 α-helices and 80 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: 17 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	103-104	2
β-strand	105-106	2	1
α-helix	113-123	11
α-helix	126-133	8
α-helix	147-165	19
β-strand	168-169	2	1
α-helix	172-181	10
α-helix	183-186	4
β-strand	188	1	2
β-strand	194	1	2
α-helix	195-196	2
α-helix	199-211	13
α-helix	215-217	3
α-helix	241-245	5
β-strand	248-256	9	3
β-strand	265	1	3
β-strand	268-271	4	3
β-strand	274-277	4	4
β-strand	284	1	5
α-helix	285-291	7
β-strand	294-295	2	3
α-helix	299	1
β-strand	300-301	2	6
β-strand	306-307	2	6
β-strand	310-315	6	3
β-strand	316	1	7
β-strand	317-318	2	3
β-strand	323-328	6	4
β-strand	330	1	8
β-strand	341	1	8
β-strand	347	1	5
β-strand	351-353	3	4
α-helix	355-357	3
β-strand	358	1	7
α-helix	360-365	6
α-helix	371-373	3
β-strand	416-426	11	4
β-strand	434-442	9	4
β-strand	445-449	5	4
β-strand	450	1	9
β-strand	453	1	9
β-strand	457	1	4
α-helix	459-462	4
α-helix	463-466	4
β-strand	473-480	8	4

Chain B: 18 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	103-104	2
β-strand	105-106	2	10
α-helix	113-123	11
α-helix	126-133	8
α-helix	147-162	16
β-strand	168-169	2	10
α-helix	172-181	10
α-helix	183-186	4
β-strand	188	1	11
β-strand	194	1	11
α-helix	195-196	2
α-helix	199-211	13
α-helix	215-217	3
α-helix	242-245	4
β-strand	248-256	9	12
β-strand	265	1	12
β-strand	268-271	4	12
β-strand	273-277	5	13
β-strand	284	1	14
α-helix	285-291	7
β-strand	294-295	2	12
α-helix	299	1
β-strand	300	1	15
α-helix	301	1
β-strand	307	1	15
β-strand	310-318	9	12
β-strand	323-328	6	13
β-strand	330	1	16
β-strand	341	1	16
β-strand	347	1	14
β-strand	351-353	3	13
α-helix	355-357	3
β-strand	358	1	12
α-helix	360-365	6
α-helix	371-373	3
β-strand	416-426	11	13
β-strand	434-442	9	13
β-strand	445-449	5	13
β-strand	450	1	17
β-strand	453	1	17
β-strand	457	1	13
α-helix	459-462	4
α-helix	463-466	4
β-strand	473-480	8	13

Chain C: 17 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	103-104	2
β-strand	105-106	2	18
α-helix	113-123	11
α-helix	126-133	8
α-helix	147-165	19
β-strand	168-169	2	18
α-helix	172-181	10
β-strand	188	1	19
β-strand	194	1	19
α-helix	195-196	2
α-helix	199-211	13
α-helix	215-217	3
α-helix	241-246	6
β-strand	248-256	9	20
β-strand	265	1	20
β-strand	268-271	4	20
β-strand	273-276	4	21
β-strand	284	1	22
α-helix	285-291	7
β-strand	294-295	2	20
α-helix	299	1
β-strand	300	1	23
α-helix	301	1
β-strand	307	1	23
β-strand	310-318	9	20
β-strand	323-327	5	21
β-strand	330	1	24
β-strand	341	1	24
β-strand	347	1	22
β-strand	351-353	3	21
α-helix	355-357	3
β-strand	358	1	20
α-helix	360-365	6
α-helix	370-373	4
β-strand	416-426	11	21
β-strand	434-442	9	21
β-strand	445-449	5	21
β-strand	450	1	25
β-strand	453	1	25
β-strand	457	1	21
α-helix	459-462	4
α-helix	463-466	4
β-strand	473-480	8	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase 14	A, B, C	protein	404	Homo sapiens	P54578 (AlphaFold model)

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

>2AYN_1 Ubiquitin carboxyl-terminal hydrolase 14 (chains A, B, C)
DMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQ
YITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRV
LQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKE
NQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVR
FFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSD
KKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKF
DDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ

Primary citation

Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. Hu, M., Li, P., Song, L. et al. EMBO J (2005) 24:3747-3756. DOI 10.1038/sj.emboj.7600832 · PubMed

Other PDB entries of the same protein (UniProt P54578 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9F6G 1.5 Å, Human USP30 chimera bound to Ubiquitin-PA
6IIK 1.97 Å, USP14 catalytic domain with IU1
6IIL 2.2 Å, USP14 catalytic domain bind to IU1-47
6IIM 2.21 Å, USP14 catalytic domain with IU1-206
6IIN 2.53 Å, USP14 catalytic domain with IU1-248
6LVS 2.73 Å, USP14 catalytic domain mutant C114S
9F19 2.75 Å, Human USP30 chimera in complex with NK036 inhibitor
7W37 3.0 Å, Structure of USP14-bound human 26S proteasome in state EA1_UBL
7W38 3.1 Å, Structure of USP14-bound human 26S proteasome in state EA2.0_UBL
7W39 3.2 Å, Structure of USP14-bound human 26S proteasome in state EA2.1_UBL
7W3G 3.2 Å, Structure of USP14-bound human 26S proteasome in substrate-engaged state ED2.0_USP14
7W3H 3.2 Å, Structure of USP14-bound human 26S proteasome in substrate-engaged state ED2.1_USP14

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