4R3Z: Human ArgRS-GlnRS-AIMP1 complex

Crystal structure of human ArgRS-GlnRS-AIMP1 complex. Determined by X-ray diffraction at 4.03 Å resolution. Released 8 Oct 2014.

Method: X-ray diffraction
Resolution: 4.03 Å
Organism: Homo sapiens
Chains: 3
Atoms: 10,242
Mol. weight: 202.16 kDa
Released: 8 Oct 2014

Explore 4R3Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4R3Z contains 57 α-helices and 56 β-strands across 3 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: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	8-15	8
α-helix	17-43	27
α-helix	48-66	19

Chain B: 39 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
α-helix	15-20	6
α-helix	22-29	8
α-helix	43-50	8
α-helix	54-65	12
α-helix	84-91	8
β-strand	102-103	2	1
β-strand	111	1	1
β-strand	113-115	3	1
α-helix	119-122	4
α-helix	134-142	9
β-strand	151-156	6	1
β-strand	162-166	5	1
α-helix	168-171	4
α-helix	173-180	8
β-strand	193-197	5	2
α-helix	201-202	2
α-helix	210-228	19
β-strand	231-235	5	2
β-strand	236	1	3
α-helix	245-255	11
α-helix	269-282	14
α-helix	285-293	9
α-helix	302-315	14
α-helix	320-326	7
β-strand	332	1	3
α-helix	335-338	4
α-helix	343-346	4
α-helix	348-351	4
β-strand	355-358	4	4
β-strand	361-364	4	4
β-strand	373-376	4	4
α-helix	387-390	4
α-helix	394-397	4
β-strand	403-407	5	2
α-helix	413-426	14
β-strand	437-439	3	2
β-strand	444-445	2	5
α-helix	460-461	2
α-helix	462-470	9
α-helix	472-475	4
α-helix	481-484	4
α-helix	487-508	22
β-strand	516-517	2	5
α-helix	531-539	9
α-helix	546-548	3
α-helix	562-565	4
α-helix	569-577	9
α-helix	581-590	10
α-helix	594-596	3
α-helix	598-601	4
α-helix	603-612	10
β-strand	618	1	6
β-strand	630	1	6
α-helix	632-635	4
α-helix	637-652	16
α-helix	654-656	3

Chain C: 15 helices, 38 β-strands

Element	Residues	Length	Sheet
α-helix	225-227	3
α-helix	249-256	8
β-strand	266-268	3	7
β-strand	277	1	8
α-helix	278-280	3
α-helix	281-293	13
β-strand	298-302	5	7
α-helix	312-325	14
β-strand	331-334	4	7
α-helix	335-338	4
α-helix	339-351	13
β-strand	355-356	2	9
α-helix	380-392	13
β-strand	402	1	10
β-strand	403-404	2	9
β-strand	418-420	3	10
β-strand	434-436	3	10
α-helix	438-448	11
β-strand	456	1	11
α-helix	464-470	7
β-strand	483	1	11
β-strand	489	1	12
α-helix	496-505	10
β-strand	518	1	8
α-helix	519-524	6
α-helix	529-538	10
β-strand	548	1	12
α-helix	551-561	11
β-strand	567	1	13
β-strand	570-571	2	14
β-strand	574-579	6	15
β-strand	591-593	3	16
β-strand	603-605	3	16
β-strand	612-615	4	15
α-helix	616-618	3
β-strand	619	1	17
β-strand	630	1	17
β-strand	631	1	18
β-strand	634	1	18
β-strand	636-637	2	19
β-strand	638	1	20
β-strand	644-645	2	19
β-strand	650-651	2	15
β-strand	660-663	4	15
β-strand	665	1	19
β-strand	678	1	20
β-strand	681-682	2	15
β-strand	688-690	3	13
β-strand	722-723	2	13
β-strand	727-728	2	14
β-strand	740-742	3	13
β-strand	747-751	5	13
β-strand	761-767	7	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1	A	protein	312	Homo sapiens	Q12904 (AlphaFold model)
Arginine--tRNA ligase, cytoplasmic	B	protein	675	Homo sapiens	P54136 (AlphaFold model)
Glutamine--tRNA ligase	C	protein	799	Homo sapiens	P47897 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4R3Z_1 Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (chains A)
MANNDAVLKRLEQKGAEADQIIEYLKQQVSLLKEKAILQATLREEKKLRVENAKLKKEIE
ELKQELIQAEIQNGVKQIPFPSGTPLHANSMVSENVIQSTAVTTVSSGTKEQIKGGTGDE
KKAKEKIEKKGEKKEKKQQSIAGSADSKPIDVSRLDLRIGCIITARKHPDADSLYVEEVD
VGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCASSPEKIEILA
PPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNDECVATYKGVPFEVKGKGV
CRAQTMSNSGIK

Sequence of entity 2 (B), FASTA

>4R3Z_2 Arginine--tRNA ligase, cytoplasmic (chains B)
MGSSHHHHHHSQDPMMDVLVSECSARLLQQEEEIKSLTAEIDRLKNCGCLGASPNLEQLQ
EENLKLKYRLNILRKSLQAERNKPTKNMINIISRLQEVFGHAIKAAYPDLENPPLLVTPS
QQAKFGDYQCNSAMGISQMLKTKEQKVNPREIAENITKHLPDNECIEKVEIAGPGFINVH
LRKDFVSEQLTSLLVNGVQLPALGENKKVIVDFSSPNIAKEMHVGHLRSTIIGESISRLF
EFAGYDVLRLNHVGDWGTQFGMLIAHLQDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEE
FKKRAYQCVVLLQGKNPDITKAWKLICDVSRQELNKIYDALDVSLIERGESFYQDRMNDI
VKEFEDRGFVQVDDGRKIVFVPGCSIPLTIVKSDGGYTYDTSDLAAIKQRLFEEKADMII
YVVDNGQSVHFQTIFAAAQMIGWYDPKVTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDL
LGEGLKRSMDKLKEKERDKVLTAEELNAAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLD
DRGNTAAYLLYAFTRIRSIARLANIDEEMLQKAARETKILLDHEKEWKLGRCILRFPEIL
QKILDDLFLHTLCDYIYELATAFTEFYDSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVM
AKGFDILGIKPVQRM

Sequence of entity 3 (C), FASTA

>4R3Z_3 Glutamine--tRNA ligase (chains C)
HGSSHHHHHHSSGLVPRGSHMASMMAALDSLSLFTSLGLSEQKARETLKNSALSAQLREA
ATQAQQTLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRS
HPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAV
LKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQ
TLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGIL
HIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYAS
DYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFS
EGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLC
TKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRL
FTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLR
VIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPV
GLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLF
QHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSH
QGKLVFNRTVTLKEDPGKV

Primary citation

Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation. Fu, Y., Kim, Y., Jin, K.S. et al. Proc Natl Acad Sci U S A (2014) 111:15084-15089. DOI 10.1073/pnas.1408836111 · PubMed

Other PDB entries of the same protein (UniProt Q12904 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1FL0 1.5 Å, Crystal structure of the EMAP2/RNA-binding domain of the P43 protein from human…
1EUJ 1.8 Å, A novel anti-tumor cytokine contains a RNA-binding motif present in aminoacyl-tRNA…
1E7Z 2.05 Å, Crystal structure of the EMAP2/RNA binding domain of the p43 protein from human…
8J9S 3.01 Å, leucine zipper complex of AIMP1 and AIMP2
8ONG Structure of the endothelial monocyte activating polypeptide II (EMAP II) in solution

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