5HBZ: EAV NSP11 K170A mutant

Structure of EAV NSP11 K170A mutant at 3.10A. Determined by X-ray diffraction at 3.1 Å resolution. Released 12 Oct 2016.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Equine arteritis virus Bucyrus
Chains: 6
Atoms: 9,946
Mol. weight: 146.17 kDa
Released: 12 Oct 2016

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

Secondary structure: helices and β-sheets

5HBZ contains 44 α-helices and 120 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: 9 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	1
α-helix	8-14	7
β-strand	18-19	2	2
β-strand	26-27	2	2
α-helix	30-33	4
β-strand	38-40	3	3
β-strand	46-51	6	3
α-helix	59	1
β-strand	60-62	3	3
β-strand	66-68	3	1
β-strand	71-73	3	1
α-helix	74-76	3
β-strand	82-88	7	3
β-strand	92-93	2	3
α-helix	94-97	4
β-strand	99	1	4
α-helix	104-107	4
α-helix	115-123	9
α-helix	125-128	4
β-strand	131-133	3	5
β-strand	136-138	3	5
β-strand	142	1	6
β-strand	157-164	8	6
β-strand	168-176	9	6
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	7
α-helix	9-13	5
β-strand	18	1	8
β-strand	26	1	8
β-strand	38-40	3	9
β-strand	47-51	5	9
α-helix	59	1
β-strand	60-62	3	9
β-strand	66-68	3	7
β-strand	71-73	3	7
α-helix	74-76	3
β-strand	82-88	7	9
β-strand	91-93	3	9
α-helix	94-97	4
β-strand	99	1	10
β-strand	101	1	11
α-helix	115-123	9
β-strand	131-133	3	12
β-strand	136-138	3	12
β-strand	142	1	13
β-strand	157-164	8	13
β-strand	168-176	9	13
β-strand	178	1	11
α-helix	180-186	7
β-strand	193-200	8	10
β-strand	203-210	8	10
β-strand	214-218	5	10

Chain C: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	14
α-helix	8-14	7
β-strand	18	1	15
β-strand	26	1	15
α-helix	30-35	6
β-strand	38-40	3	16
β-strand	47-51	5	16
α-helix	59	1
β-strand	60-62	3	16
β-strand	66-68	3	14
β-strand	71-73	3	14
β-strand	82-88	7	16
β-strand	91-92	2	16
α-helix	94-97	4
β-strand	99	1	17
α-helix	104-107	4
α-helix	115-123	9
α-helix	125-128	4
β-strand	131-133	3	18
β-strand	136-138	3	18
β-strand	142	1	19
β-strand	157-164	8	19
β-strand	168-176	9	19
α-helix	180-186	7
β-strand	193-200	8	17
β-strand	203-210	8	17
β-strand	214-218	5	17

Chain D: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	20
α-helix	8-13	6
β-strand	18	1	21
β-strand	26	1	21
α-helix	30-32	3
β-strand	38-40	3	22
β-strand	47-51	5	22
α-helix	59	1
β-strand	60-62	3	22
β-strand	66-68	3	20
β-strand	71-73	3	20
α-helix	74-76	3
β-strand	82-88	7	22
β-strand	91-93	3	22
β-strand	99	1	23
β-strand	101	1	24
α-helix	105-107	3
α-helix	115-123	9
β-strand	128-132	5	23
β-strand	137-138	2	23
β-strand	140-142	3	25
β-strand	157	1	25
β-strand	174-176	3	25
β-strand	178	1	24
α-helix	180-183	4
β-strand	193-200	8	23
β-strand	203-210	8	23
β-strand	214-218	5	23

Chain E: 6 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	26
α-helix	8-13	6
β-strand	18-19	2	27
β-strand	26-27	2	27
α-helix	30-33	4
β-strand	38-40	3	28
β-strand	47-51	5	28
α-helix	59	1
β-strand	60-62	3	28
β-strand	66-68	3	26
β-strand	71-73	3	26
β-strand	82-88	7	28
β-strand	91-93	3	28
β-strand	99	1	29
α-helix	105-107	3
α-helix	115-123	9
β-strand	128-132	5	29
β-strand	138	1	29
β-strand	140-142	3	30
β-strand	157	1	30
β-strand	174-176	3	30
α-helix	180-183	4
β-strand	193-200	8	29
β-strand	203-210	8	29
β-strand	214-218	5	29

Chain F: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	31
α-helix	8-13	6
β-strand	18-19	2	32
β-strand	26-27	2	32
α-helix	30-33	4
β-strand	38-40	3	32
β-strand	47-51	5	32
α-helix	59	1
β-strand	60-62	3	32
β-strand	66-68	3	31
β-strand	71-73	3	31
α-helix	74-76	3
β-strand	82-88	7	32
β-strand	91-93	3	32
α-helix	94	1
β-strand	99	1	33
β-strand	101	1	34
α-helix	105-107	3
α-helix	115-123	9
β-strand	128-132	5	33
β-strand	138	1	33
β-strand	140-142	3	35
β-strand	157	1	35
β-strand	174-176	3	35
β-strand	178	1	34
α-helix	180-186	7
β-strand	193-200	8	33
β-strand	203-210	8	33
β-strand	214-218	5	33

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Non-structural protein 11	A, B, C, D, E, F	protein	221	Equine arteritis virus Bucyrus	P19811 (AlphaFold model)

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

>5HBZ_1 Non-structural protein 11 (chains A, B, C, D, E, F)
ESSNKISCLPRVAQNLGYHYSPDLPGFCPIPKELAEHWPVVSNDRYPNCLQITLQQVCEL
SKPCSAGYMVGQSVFVQTPGVTSYWLTEWVDGKARALPDSLFSSGRFETNSRAFLDEAEE
KFAAAHPHACLGEINKSTVGGSHFIFSQYLPPLLPADAVALVGASLAGKAAAAACSVVDV
YAPSFEPYLHPETLSRVYKIMIDFKPCRLMVWRNATFYVQE

Primary citation

Structural Biology of the Arterivirus nsp11 Endoribonucleases. Zhang, M., Li, X., Deng, Z. et al. J Virol (2017) 91. DOI 10.1128/JVI.01309-16 · PubMed

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
5HC1 3.1 Å, Structure of EAV NSP11 H141A mutant at 3.10A
5F17 3.2 Å, Structure of EAV NSP11 K170A mutant at 3.19A
2L8K NMR Structure of the Arterivirus nonstructural protein 7 alpha (nsp7 alpha)

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