2AYO: USP14

Structure of USP14 bound to ubquitin aldehyde. Determined by X-ray diffraction at 3.5 Å resolution. Released 18 Oct 2005.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,411
Mol. weight: 54.77 kDa
Released: 18 Oct 2005

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

Secondary structure: helices and β-sheets

2AYO contains 15 α-helices and 29 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: 12 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	105	1	1
α-helix	113-123	11
α-helix	126-133	8
α-helix	148-162	15
β-strand	168	1	1
α-helix	173-181	9
β-strand	198	1	2
α-helix	199-213	15
α-helix	215-217	3
α-helix	241-245	5
β-strand	249-256	8	3
β-strand	265-269	5	3
β-strand	273-275	3	4
β-strand	284	1	5
α-helix	285-288	4
β-strand	296-300	5	3
β-strand	307-318	12	3
β-strand	323-326	4	4
β-strand	347	1	5
β-strand	351-352	2	4
α-helix	355-357	3
β-strand	358	1	3
α-helix	362-366	5
α-helix	367-371	5
β-strand	417-421	5	4
β-strand	422-427	6	6
β-strand	433-438	6	6
β-strand	439-440	2	7
β-strand	446-450	5	7
β-strand	453-457	5	7
α-helix	459-462	4
β-strand	474	1	6
β-strand	476-480	5	4

Chain B: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	8
β-strand	12-16	5	8
β-strand	22	1	9
α-helix	23-34	12
α-helix	38-40	3
β-strand	42-45	4	8
β-strand	48-49	2	8
α-helix	50-51	2
β-strand	55	1	9
β-strand	66-70	5	8
β-strand	74	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase 14	A	protein	404	Homo sapiens	P54578 (AlphaFold model)
Ubiquitin	B	protein	76	Homo sapiens	P0CG48 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2AYO_1 Ubiquitin carboxyl-terminal hydrolase 14 (chains A)
DMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQ
YITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRV
LQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKE
NQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVR
FFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSD
KKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKF
DDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ

Sequence of entity 2 (B), FASTA

>2AYO_2 Ubiquitin (chains B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

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
2AYN 3.2 Å, Structure of USP14, a proteasome-associated deubiquitinating enzyme
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

Browse structure collections

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