1g3i

X-ray diffraction
3.41Å resolution

CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero 24-mer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent protease ATPase subunit HslU Chains: A, B, C, D, E, F, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, S, T, U, V, W, X
Length: 444 amino acids
Theoretical weight: 49.44 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P43773 (Residues: 1-444; Coverage: 100%)
Gene names: HI_0497, hslU
Sequence domains:
Structure domains:
ATP-dependent protease subunit HslV Chains: G, H, I, J, K, L, M, N, O, P, Q, R
Molecule details ›
Chains: G, H, I, J, K, L, M, N, O, P, Q, R
Length: 174 amino acids
Theoretical weight: 18.9 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P43772 (Residues: 2-175; Coverage: 99%)
Gene names: HI_0496, hslV
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21212
Unit cell:
a: 209.223Å b: 220.579Å c: 241.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.284
Expression system: Escherichia coli BL21(DE3)