5F17: EAV NSP11 K170A mutant

Structure of EAV NSP11 K170A mutant at 3.19A. Determined by X-ray diffraction at 3.2 Å resolution. Released 16 Nov 2016.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Equine arteritis virus Bucyrus
Chains: 6
Atoms: 9,879
Mol. weight: 144.87 kDa
Released: 16 Nov 2016

Explore 5F17 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5F17 contains 35 α-helices and 122 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: 5 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	1
α-helix	8-13	6
β-strand	18	1	2
β-strand	26	1	2
β-strand	38-40	3	3
β-strand	46-51	6	3
β-strand	60-62	3	3
β-strand	66-68	3	1
β-strand	71-73	3	1
β-strand	82-88	7	3
β-strand	91-93	3	3
β-strand	99	1	4
β-strand	101	1	5
α-helix	104-107	4
α-helix	115-123	9
α-helix	125-128	4
β-strand	131-132	2	6
β-strand	137-138	2	6
β-strand	142	1	7
β-strand	157-164	8	7
β-strand	168-176	9	7
β-strand	178	1	5
α-helix	180-186	7
β-strand	193-200	8	4
β-strand	203-210	8	4
β-strand	214-218	5	4

Chain B: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	8
α-helix	9-13	5
β-strand	18	1	9
β-strand	26	1	9
β-strand	38-40	3	10
β-strand	47-51	5	10
α-helix	59	1
β-strand	60-62	3	10
β-strand	66-68	3	8
β-strand	71-73	3	8
β-strand	82-88	7	10
β-strand	91-93	3	10
α-helix	94-97	4
β-strand	99	1	11
β-strand	101	1	12
α-helix	115-123	9
α-helix	125-128	4
β-strand	131-132	2	13
β-strand	137-138	2	13
β-strand	142	1	14
β-strand	157-164	8	14
β-strand	168-176	9	14
β-strand	178	1	12
α-helix	180-183	4
β-strand	193-200	8	11
β-strand	203-210	8	11
β-strand	214-218	5	11

Chain C: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	15
α-helix	8-12	5
β-strand	18	1	16
β-strand	26	1	16
α-helix	30-35	6
β-strand	38-40	3	17
β-strand	47-51	5	17
α-helix	59	1
β-strand	60-62	3	17
β-strand	66-68	3	15
β-strand	71-73	3	15
β-strand	82-88	7	17
β-strand	91-92	2	17
α-helix	94-97	4
β-strand	99	1	18
β-strand	101	1	19
α-helix	104-107	4
α-helix	115-123	9
β-strand	131-132	2	20
β-strand	137-138	2	20
β-strand	142	1	21
β-strand	157-164	8	21
β-strand	168-176	9	21
β-strand	178	1	19
α-helix	180-183	4
β-strand	193-200	8	18
β-strand	203-210	8	18
β-strand	214-218	5	18

Chain D: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	22
α-helix	8-12	5
β-strand	18-19	2	23
β-strand	26-27	2	23
α-helix	30-35	6
β-strand	38-40	3	23
β-strand	47-51	5	23
α-helix	59	1
β-strand	60-62	3	23
β-strand	66-68	3	22
β-strand	71-73	3	22
β-strand	82-88	7	23
β-strand	91-93	3	23
β-strand	99	1	24
β-strand	101	1	25
α-helix	104-107	4
α-helix	115-123	9
β-strand	131-132	2	24
β-strand	137-138	2	24
β-strand	140-142	3	26
β-strand	157-158	2	26
β-strand	174-176	3	26
β-strand	178	1	25
α-helix	180-183	4
β-strand	193-200	8	24
β-strand	203-210	8	24
β-strand	215-218	4	24

Chain E: 6 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	27
α-helix	9-13	5
β-strand	18-19	2	28
β-strand	26-27	2	28
α-helix	31-35	5
β-strand	39-40	2	29
β-strand	47-51	5	29
α-helix	59	1
β-strand	60-62	3	29
β-strand	66-68	3	27
β-strand	71-73	3	27
β-strand	82-88	7	29
β-strand	91-93	3	29
β-strand	99	1	30
β-strand	101	1	31
α-helix	105-107	3
α-helix	115-123	9
β-strand	140-142	3	32
β-strand	157	1	32
β-strand	174-176	3	32
β-strand	178	1	31
α-helix	180-183	4
β-strand	193-200	8	30
β-strand	203-210	8	30
β-strand	214-217	4	30

Chain F: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	33
α-helix	8-12	5
β-strand	18-19	2	34
β-strand	26-27	2	34
α-helix	30-35	6
β-strand	38-40	3	34
β-strand	47-51	5	34
β-strand	60-62	3	34
β-strand	66-68	3	33
β-strand	71-73	3	33
β-strand	82-88	7	34
β-strand	91-93	3	34
β-strand	99	1	35
β-strand	101	1	36
α-helix	105-107	3
α-helix	115-123	9
β-strand	141-142	2	37
β-strand	175-176	2	37
β-strand	178	1	36
α-helix	180-186	7
β-strand	193-200	8	35
β-strand	203-210	8	35
β-strand	215	1	35
β-strand	218	1	35

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Non-structural protein 11	A, B, C, D, E, F	protein	219	Equine arteritis virus Bucyrus	P19811 (AlphaFold model)

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

>5F17_1 Non-structural protein 11 (chains A, B, C, D, E, F)
SNKISCLPRVAQNLGYHYSPDLPGFCPIPKELAEHWPVVSNDRYPNCLQITLQQVCELSK
PCSAGYMVGQSVFVQTPGVTSYWLTEWVDGKARALPDSLFSSGRFETNSRAFLDEAEEKF
AAAHPHACLGEINKSTVGGSHFIFSQYLPPLLPADAVALVGASLAGKAAAAACSVVDVYA
PSFEPYLHPETLSRVYKIMIDFKPCRLMVWRNATFYVQE

Primary citation

Structure of EAV NSP11 K170A mutant at 3.19A. Zhang, M.F., Chen, Z.Z. To be published.

Other PDB entries of the same protein (UniProt P19811 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4IUM 1.45 Å, Equine arteritis virus papain-like protease 2 (PLP2) covalently bound to ubiquitin
1MBM 2.0 Å, NSP4 proteinase from Equine Arteritis Virus
4N0N 2.0 Å, Crystal structure of Arterivirus nonstructural protein 10 (helicase)
4N0O 2.65 Å, Complex structure of Arterivirus nonstructural protein 10 (helicase) with DNA
5HBZ 3.1 Å, Structure of EAV NSP11 K170A mutant at 3.10A
5HC1 3.1 Å, Structure of EAV NSP11 H141A mutant at 3.10A
2L8K NMR Structure of the Arterivirus nonstructural protein 7 alpha (nsp7 alpha)

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