6LVS: USP14 catalytic domain mutant C114S

USP14 catalytic domain mutant C114S. Determined by X-ray diffraction at 2.73 Å resolution. Released 18 Mar 2020.

Method: X-ray diffraction
Resolution: 2.73 Å
Organism: Homo sapiens
Chains: 6
Atoms: 16,510
Mol. weight: 285.9 kDa
Released: 18 Mar 2020

Explore 6LVS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6LVS contains 98 α-helices and 148 β-strands across 6 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: 16 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	106-107	2	1
α-helix	114-123	10
α-helix	127-134	8
α-helix	147-164	18
β-strand	169-170	2	1
α-helix	173-182	10
α-helix	184-186	3
β-strand	189	1	2
α-helix	194	1
β-strand	195	1	2
α-helix	196-197	2
α-helix	200-211	12
β-strand	216	1	3
α-helix	217-218	2
β-strand	241	1	3
α-helix	242-247	6
β-strand	249-257	9	4
α-helix	264-265	2
β-strand	266-272	7	4
β-strand	275-277	3	5
β-strand	285	1	6
α-helix	286-294	9
β-strand	295-302	8	4
β-strand	307-319	13	4
β-strand	321	1	7
β-strand	324-328	5	5
β-strand	331-334	4	8
β-strand	339-342	4	8
β-strand	348	1	6
β-strand	352-354	3	5
α-helix	356-358	3
β-strand	359	1	4
α-helix	361-368	8
β-strand	406	1	9
β-strand	409	1	9
β-strand	412	1	7
β-strand	417-427	11	5
β-strand	435-443	9	5
β-strand	446-451	6	5
β-strand	454-458	5	5
α-helix	460-464	5
α-helix	465-467	3
β-strand	474-482	9	5

Chain B: 16 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	106-107	2	10
α-helix	114-123	10
α-helix	127-135	9
α-helix	147-164	18
β-strand	169-170	2	10
α-helix	173-182	10
α-helix	184-186	3
β-strand	189	1	11
α-helix	194	1
β-strand	195	1	11
α-helix	196-197	2
α-helix	200-212	13
β-strand	216	1	12
α-helix	217-218	2
β-strand	241	1	12
α-helix	242-247	6
β-strand	249-257	9	13
α-helix	264-265	2
β-strand	266-272	7	13
β-strand	275-277	3	14
β-strand	285	1	15
α-helix	286-294	9
β-strand	295-302	8	13
β-strand	307-319	13	13
β-strand	321	1	16
β-strand	324-328	5	14
β-strand	331-334	4	17
β-strand	339-342	4	17
β-strand	348	1	15
β-strand	352-354	3	14
α-helix	356-358	3
β-strand	359	1	13
α-helix	361-368	8
β-strand	406	1	18
β-strand	409	1	18
β-strand	412	1	16
β-strand	417-427	11	14
β-strand	435-441	7	14
β-strand	447-451	5	14
β-strand	454-458	5	14
α-helix	460-464	5
α-helix	465-467	3
β-strand	474-482	9	14

Chain C: 17 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	103-105	3
β-strand	106-107	2	19
α-helix	114-123	10
α-helix	127-135	9
α-helix	147-164	18
β-strand	169-170	2	19
α-helix	173-182	10
α-helix	184-187	4
β-strand	189	1	20
β-strand	195	1	20
α-helix	196-197	2
α-helix	200-212	13
α-helix	216-218	3
α-helix	242-247	6
β-strand	249-257	9	4
α-helix	264-265	2
β-strand	266-272	7	4
β-strand	275-277	3	21
β-strand	285	1	22
α-helix	286-294	9
β-strand	295-301	7	4
β-strand	308-319	12	4
β-strand	321	1	23
β-strand	324-328	5	21
β-strand	331-334	4	24
α-helix	335-337	3
β-strand	339-342	4	24
β-strand	348	1	22
β-strand	352-354	3	21
α-helix	356-358	3
β-strand	359	1	4
α-helix	361-371	11
β-strand	406	1	25
β-strand	409	1	25
β-strand	412	1	23
β-strand	417-427	11	21
β-strand	435-443	9	21
β-strand	446-451	6	21
β-strand	454-458	5	21
α-helix	460-464	5
α-helix	465-467	3
β-strand	474-482	9	21

Chain D: 19 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	106-107	2	26
α-helix	114-123	10
α-helix	127-135	9
α-helix	148-164	17
β-strand	169-170	2	26
α-helix	173-182	10
α-helix	184-186	3
α-helix	188	1
β-strand	189	1	27
α-helix	190	1
β-strand	195	1	27
α-helix	196-197	2
α-helix	200-212	13
α-helix	216-218	3
α-helix	242-247	6
β-strand	249-257	9	28
α-helix	264-265	2
β-strand	266-272	7	28
β-strand	275-277	3	29
β-strand	285	1	30
α-helix	286-294	9
β-strand	295-302	8	28
β-strand	307-319	13	28
β-strand	321	1	31
β-strand	324-328	5	29
β-strand	331-334	4	32
α-helix	335-337	3
β-strand	339-342	4	32
β-strand	348	1	30
β-strand	352-354	3	29
α-helix	356-358	3
β-strand	359	1	28
α-helix	361-368	8
α-helix	369-371	3
β-strand	412	1	31
β-strand	417-427	11	29
β-strand	435-443	9	29
β-strand	446-451	6	29
β-strand	454-458	5	29
α-helix	460-463	4
α-helix	464-467	4
β-strand	474-481	8	29

Chain E: 14 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	106-107	2	33
α-helix	114-123	10
α-helix	127-134	8
α-helix	148-163	16
β-strand	169-170	2	33
α-helix	173-182	10
α-helix	184-187	4
β-strand	189	1	34
α-helix	194	1
β-strand	195	1	34
α-helix	196-197	2
α-helix	200-212	13
α-helix	216-218	3
α-helix	242-247	6
β-strand	249-257	9	35
β-strand	266-272	7	35
β-strand	275-277	3	36
β-strand	285	1	37
α-helix	286-292	7
β-strand	295-302	8	35
β-strand	307-319	13	35
β-strand	321	1	38
β-strand	324-328	5	36
β-strand	331-332	2	39
β-strand	341-342	2	39
β-strand	348	1	37
β-strand	352-354	3	36
α-helix	356-358	3
β-strand	359	1	35
α-helix	361-371	11
β-strand	412	1	38
β-strand	417-427	11	36
β-strand	435-443	9	36
β-strand	446-451	6	36
β-strand	454-458	5	36
α-helix	460-464	5
β-strand	474-482	9	36

Chain F: 16 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	106-107	2	40
α-helix	114-124	11
α-helix	127-134	8
α-helix	145-147	3
α-helix	148-164	17
β-strand	169-170	2	40
α-helix	173-182	10
α-helix	184-187	4
β-strand	189	1	41
α-helix	194	1
β-strand	195	1	41
α-helix	196-197	2
α-helix	200-211	12
α-helix	216-218	3
α-helix	242-247	6
β-strand	249-257	9	42
α-helix	264-265	2
β-strand	266-272	7	42
β-strand	275-277	3	43
β-strand	285	1	44
α-helix	286-293	8
β-strand	295-301	7	42
β-strand	308-319	12	42
β-strand	321	1	45
β-strand	324-328	5	43
β-strand	331	1	46
β-strand	342	1	46
β-strand	348	1	44
β-strand	352-354	3	43
α-helix	356-358	3
β-strand	359	1	42
α-helix	361-368	8
β-strand	412	1	45
β-strand	417-427	11	43
β-strand	435-443	9	43
β-strand	446-451	6	43
β-strand	454-458	5	43
α-helix	460-464	5
β-strand	474-482	9	43

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase 14	A, B, C, D, E, F	protein	410	Homo sapiens	P54578 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>6LVS_1 Ubiquitin carboxyl-terminal hydrolase 14 (chains A, B, C, D, E, F)
HHHHHHSSGLVPRGSHMTEEQLASAMELPCGLTNLGNTSYMNATVQCIRSVPELKDALKR
YAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQY
LQQDANECWIQMMRVLQQKLEAIEDDSSAATPSKKKSLIDQFFGVEFETTMKCTESEEEE
VTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYL
TIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQ
QPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQ
DEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ

Primary citation

USP14 catalytic domain mutant C114S. Lin, H.C. To be published.

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
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
7W3H 3.2 Å, Structure of USP14-bound human 26S proteasome in substrate-engaged state ED2.1_USP14

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