› 6k0o

X-ray diffraction
1.99Å resolution

The crystal structure of human CD163-like homolog SRCR8

Released:
DOI: 10.2210/pdb6k0o/pdb
PDB entry 6k0o coloured by chain, front view.
PDB entry 6k0o coloured by chain, side view.
PDB entry 6k0o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural comparison of CD163 SRCR5 from different species sheds some light on its involvement in porcine reproductive and respiratory syndrome virus-2 infection in vitro.
Ma H, Li R, Jiang L, Qiao S, Chen XX, Wang A, Zhang G
OpenAccess logo Vet Res 52 97 (2021)
PMID: 34193250

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192527 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Scavenger receptor cysteine-rich type 1 protein M160 Chains: A, B
Molecule details ›
Chains: A, B
Length: 104 amino acids
Theoretical weight: 11.27 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: Q9NR16 (Residues: 795-895; Coverage: 7%)
Gene names: CD163B, CD163L1, M160, UNQ6434/PRO23202
Sequence domains: Scavenger receptor cysteine-rich domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: C2
Unit cell:
a: 29.497Å b: 73.043Å c: 82.74Å
α: 90° β: 89.96° γ: 90°
R-values:
R R work R free
0.199 0.195 0.269
Expression system: Drosophila melanogaster

Quick links

Citations

2 review citations

Reappraising host cellular factors involved in attachment and entry to develop antiviral strategies against porcine reproductive and respiratory syndrome virus.
Li et al. (2022)
1 more

1 mention without citation

Structural comparison of CD163 SRCR5 from different species sheds some light on its involvement in porcine reproductive and respiratory syndrome virus-2 infection in vitro.
Ma et al. (2021)