5nbm

X-ray diffraction
3.4Å resolution

Crystal structure of the Arp4-N-actin(ATP-state) heterodimer bound by a nanobody

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Actin-related protein 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 489 amino acids
Theoretical weight: 54.89 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P80428 (Residues: 1-489; Coverage: 100%)
Gene names: ACT3, ARP4, J1012, YJL081C
Sequence domains: Actin
Structure domains:
Actin Chains: C, D
Molecule details ›
Chains: C, D
Length: 375 amino acids
Theoretical weight: 41.75 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P60010 (Residues: 1-375; Coverage: 100%)
Gene names: ABY1, ACT1, END7, YFL039C
Sequence domains: Actin
Structure domains:
nAct-Nanobody Chains: E, F
Molecule details ›
Chains: E, F
Length: 159 amino acids
Theoretical weight: 17.16 KDa
Source organism: Vicugna pacos
Expression system: Escherichia coli
Unknown peptide Chains: G, H
Molecule details ›
Chains: G, H
Length: 17 amino acids
Theoretical weight: 1.46 KDa
Source organism: Trichoplusia ni
Expression system: Trichoplusia ni

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P65
Unit cell:
a: 190.581Å b: 190.581Å c: 220.616Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.154 0.152 0.193
Expression systems:
  • Trichoplusia ni
  • Escherichia coli