4YNV: Assembly Chaperone of RpL4 (Acl4)

Name: PDB 4YNV: Assembly Chaperone of RpL4 (Acl4) (Residues 28-338)
Published: 2015-05-13
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Assembly Chaperone of RpL4 (Acl4) (Residues 28-338). Determined by X-ray diffraction at 2.95 Å resolution. Released 13 May 2015.

Method: X-ray diffraction
Resolution: 2.95 Å
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Chains: 2
Atoms: 4,432
Mol. weight: 70.62 kDa
Released: 13 May 2015

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

Secondary structure: helices and β-sheets

4YNV contains 29 α-helices and 0 β-strands across 2 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: 15 helices, 0 β-strands

Element	Residues	Length
α-helix	30-42	13
α-helix	46-60	15
α-helix	67-81	15
α-helix	84-97	14
α-helix	105-108	4
α-helix	112-120	9
α-helix	125-152	28
α-helix	158-183	26
α-helix	191-206	16
α-helix	211-223	13
α-helix	227-238	12
α-helix	252-253	2
α-helix	254-267	14
α-helix	270-283	14
α-helix	289-309	21

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	30-42	13
α-helix	46-60	15
α-helix	67-81	15
α-helix	84-97	14
α-helix	112-120	9
α-helix	125-152	28
α-helix	158-183	26
α-helix	191-206	16
α-helix	211-223	13
α-helix	227-238	12
α-helix	252-253	2
α-helix	254-267	14
α-helix	270-283	14
α-helix	289-309	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ACL4	A, B	protein	312	Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)	G0S0I4 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4YNV_1 ACL4 (chains A, B)
SINPKELLDRATTLLEEGDIETAAKVARTAYEHIGENGRHAGAALTLLGQIHVELGDIDA
ARNYYAAAVKVDEDGSLPEELGGGPEKFLWLAQLSEEGGHDSVAWFERGATVLRAQIQSL
MDSLEQRPLSRGQVEAAIADKRRRLAETLCAVVEVYMTDLSWEDDAEQRCEALITEATMI
APEWPETWQTVANVRISQERTEEAREALRRSLGLWTHLPPEDPGVPPFPSRVSLVRLLIE
VDMEEEALEVTERLIAEDDLSVEVWYLGGYARYRLGEKEREASGQASEPEAWKDTWRSSR
KWLRQCLKVFEA

Primary citation

Coordinated Ribosomal L4 Protein Assembly into the Pre-Ribosome Is Regulated by Its Eukaryote-Specific Extension. Stelter, P., Huber, F.M., Kunze, R. et al. Mol Cell (2015) 58:854-862. DOI 10.1016/j.molcel.2015.03.029 · PubMed

Other PDB entries of the same protein (UniProt G0S0I4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5TQB 2.4 Å, Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with…
4YNW 2.95 Å, Assembly Chaperone of RpL4 (Acl4) (Residues 1-338)

Browse structure collections

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