4TXQ: LIP5 N-terminal domain

Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM. Determined by X-ray diffraction at 2.21 Å resolution. Released 11 Feb 2015.

Method: X-ray diffraction
Resolution: 2.21 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,008
Mol. weight: 43.02 kDa
Released: 11 Feb 2015

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

Secondary structure: helices and β-sheets

4TXQ contains 25 α-helices and 0 β-strands across 4 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	5-7	3
α-helix	9-11	3
α-helix	12-17	6
α-helix	18-27	10
α-helix	32-49	18
α-helix	54-74	21
α-helix	78-81	4
α-helix	83-107	25
α-helix	112-128	17
α-helix	129-131	3
α-helix	133-135	3
α-helix	136-157	22

Chain B: 11 helices, 0 β-strands

Element	Residues	Length
α-helix	6-11	6
α-helix	12-17	6
α-helix	18-27	10
α-helix	32-49	18
α-helix	54-73	20
α-helix	78-81	4
α-helix	83-106	24
α-helix	112-127	16
α-helix	128-131	4
α-helix	134-135	2
α-helix	136-157	22

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	187-195	9

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	184-197	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vacuolar protein sorting-associated protein VTA1 homolog	A, B	protein	163	Homo sapiens	Q9NP79 (AlphaFold model)
Charged multivesicular body protein 1b	C, D	protein	25	Homo sapiens	Q7LBR1 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4TXQ_1 Vacuolar protein sorting-associated protein VTA1 homolog (chains A, B)
SMAALAPLPPLPAQFKSIQHHLRTAQEHDKRDPVVAYYCRLYAMQTGMKIDSKTPECRKF
LSKLMDQLEALKKQLGDNEAITQEIVGCAHLENYALKMFLYADNEDRAGRFHKNMIKSFY
TASLLIDVITVFGELTDENVKHRKYARWKATYIHNCLKNGETP

Sequence of entity 2 (C, D), FASTA

>4TXQ_2 Charged multivesicular body protein 1b (chains C, D)
SVGTSVASAEQDELSQRLARLRDQV

Primary citation

A Novel Mechanism of Regulating the ATPase VPS4 by Its Cofactor LIP5 and the Endosomal Sorting Complex Required for Transport (ESCRT)-III Protein CHMP5. Vild, C.J., Li, Y., Guo, E.Z. et al. J Biol Chem (2015) 290:7291-7303. DOI 10.1074/jbc.M114.616730 · PubMed

Other PDB entries of the same protein (UniProt Q9NP79 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4TXR 1.0 Å, Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM and CHMP5 MIM
4U7E 1.6 Å, The crystal structure of the complex of LIP5 NTD and IST1 MIM
4TXP 3.01 Å, Crystal structure of LIP5 N-terminal domain
2LXL Lip5(mit)2
2LXM Lip5-chmp5

Browse structure collections

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