5BMU: PDB entry 5BMU

The crystal structure of the GST-like domains complex of AIMP3-EPRS mutant C92SC105SC123S. Determined by X-ray diffraction at 2.6 Å resolution. Released 21 Oct 2015.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 8
Atoms: 10,463
Mol. weight: 154.96 kDa
Released: 21 Oct 2015

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

Secondary structure: helices and β-sheets

5BMU contains 79 α-helices and 38 β-strands across 8 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: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
β-strand	18	1	1
β-strand	23-25	3	2
β-strand	30-33	4	2
β-strand	41-42	2	2
α-helix	44-54	11
α-helix	58-61	4
α-helix	65-77	13
α-helix	78-82	5
α-helix	92-102	11
α-helix	115-129	15
α-helix	133-138	6
α-helix	140-150	11
α-helix	159-163	5

Chain B: 8 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	3
α-helix	17-23	7
β-strand	30-34	5	3
β-strand	39-41	3	3
β-strand	47-48	2	3
α-helix	51-61	11
α-helix	72-88	17
α-helix	95-105	11
β-strand	111	1	4
β-strand	114	1	4
α-helix	119-130	12
α-helix	132-139	8
α-helix	145-156	12
α-helix	158-166	9

Chain C: 11 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
β-strand	23-25	3	5
β-strand	30-33	4	5
β-strand	41-42	2	5
α-helix	44-54	11
α-helix	58-61	4
α-helix	65-77	13
α-helix	78-82	5
α-helix	92-101	10
α-helix	102-104	3
β-strand	107	1	6
β-strand	110	1	6
α-helix	115-130	16
α-helix	135-138	4
α-helix	140-150	11
α-helix	159-163	5

Chain D: 8 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	7
α-helix	17-22	6
β-strand	30-35	6	7
β-strand	39-41	3	7
β-strand	47-48	2	7
α-helix	51-61	11
α-helix	72-86	15
α-helix	95-106	12
β-strand	111	1	8
β-strand	114	1	8
α-helix	119-130	12
α-helix	132-137	6
α-helix	145-155	11
α-helix	158-167	10

Chain E: 11 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
β-strand	18	1	1
β-strand	23-25	3	9
β-strand	30-32	3	9
β-strand	33	1	10
α-helix	40	1
β-strand	41	1	10
α-helix	44-54	11
α-helix	58-60	3
α-helix	65-77	13
α-helix	78-82	5
α-helix	92-101	10
α-helix	115-129	15
α-helix	133-138	6
α-helix	140-150	11
α-helix	160-161	2

Chain F: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	11
α-helix	15-22	8
α-helix	25-27	3
β-strand	30-34	5	11
β-strand	39-40	2	11
β-strand	48	1	11
α-helix	51-61	11
α-helix	72-87	16
α-helix	88-90	3
α-helix	95-105	11
α-helix	119-129	11
α-helix	132-140	9
α-helix	145-155	11
α-helix	158-166	9

Chain G: 12 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
α-helix	19-21	3
β-strand	23-25	3	12
β-strand	30-33	4	12
β-strand	41-42	2	12
α-helix	44-54	11
α-helix	58-60	3
α-helix	65-77	13
α-helix	78-82	5
α-helix	85-89	5
α-helix	91-101	11
α-helix	115-130	16
α-helix	133-138	6
α-helix	140-150	11
α-helix	160-161	2

Chain H: 9 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	13
β-strand	8	1	14
α-helix	17-22	6
β-strand	34	1	14
β-strand	39-42	4	13
β-strand	46-48	3	13
α-helix	51-61	11
α-helix	72-87	16
α-helix	95-105	11
α-helix	106-108	3
α-helix	119-129	11
α-helix	132-140	9
α-helix	145-156	12
α-helix	158-166	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Eukaryotic translation elongation factor 1 epsilon-1	A, C, E, G	protein	171	Homo sapiens	O43324 (AlphaFold model)
Glutamate--tRNA ligase	B, D, F, H	protein	175	Homo sapiens	P07814 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>5BMU_1 Eukaryotic translation elongation factor 1 epsilon-1 (chains A, C, E, G)
GHMAAAAELSLLEKSLGLSKGNKYSAQGERQIPVLQTNNGPSLTGLTTIAAHLVKQANKE
YLLGSTAEEKAIVQQWLEYRVTQVDGHSSKNDIHTLLKDLNSYLEDKVYLTGYNFTLADI
LLYYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRL

Sequence of entity 2 (B, D, F, H), FASTA

>5BMU_2 Glutamate--tRNA ligase (chains B, D, F, H)
MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLAR
VATTAGLYGSNLMEHTEIDHWLEFSATKLSSSDSFTSTINELNHSLSLRTYLVGNSLSLA
DLSVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKAR

Primary citation

Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains. Cho, H.Y., Maeng, S.J., Cho, H.J. et al. J Biol Chem (2015) 290:29313-29328. DOI 10.1074/jbc.M115.690867 · PubMed

Other PDB entries of the same protein (UniProt O43324 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4BVX 1.6 Å, Crystal structure of the AIMP3-MRS N-terminal domain complex with I3C
4BL7 1.89 Å, Crystal structure of the AIMP3-MRS N-terminal domain complex in different space group
4BVY 1.99 Å, Crystal structure of the AIMP3-MRS N-terminal domain complex
2UZ8 2.0 Å, The crystal structure of p18, human translation elongation factor 1 epsilon 1
5Y6L 2.9 Å, A subcomplex crystal structure of human cytosolic aspartyl-tRNA synthetase and…

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