› 1p63

X-ray diffraction
1.6Å resolution

Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)

Released:
DOI: 10.2210/pdb1p63/pdb
PDB entry 1p63 coloured by chain, front view.
PDB entry 1p63 coloured by chain, side view.
PDB entry 1p63 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Accommodation of a highly symmetric core within a symmetric protein superfold.
Brych SR, Kim J, Logan TM, Blaber M
Protein Sci 12 2704-18 (2003)
PMID: 14627732

Function and Biology Details

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

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: 144 amino acids
Theoretical weight: 16.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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 SO4 1 x SO4
Ligand FMT 1 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2221
Unit cell:
a: 74.41Å b: 96.72Å c: 107.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.219 0.251
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Emergence of symmetric protein architecture from a simple peptide motif: evolutionary models.
Blaber et al. (2012)
16 other articles

1 mention without citation

Accommodation of a highly symmetric core within a symmetric protein superfold.
Brych et al. (2003)