› 4q91

X-ray diffraction
1.8Å resolution

Crystal structure of C16A/K12V/C117V/P134V mutant of human acidic fibroblast growth factor

Released:
DOI: 10.2210/pdb4q91/pdb
PDB entry 4q91 coloured by chain, front view.
PDB entry 4q91 coloured by chain, side view.
PDB entry 4q91 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mutation choice to eliminate buried free cysteines in protein therapeutics.
Xia X, Longo LM, Blaber M
J Pharm Sci 104 566-76 (2015)
PMID: 25312595

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fibroblast growth factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 146 amino acids
Theoretical weight: 16.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05230 (Residues: 16-155; Coverage: 90%)
Gene names: FGF1, FGFA
Sequence domains: Fibroblast growth factor
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

2 bound ligands:
Ligand FMT 5 x FMT
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2221
Unit cell:
a: 74.138Å b: 97.104Å c: 108.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.186
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Engineering protein-based therapeutics through structural and chemical design.
Ebrahimi et al. (2023)
8 other articles