› 1m16

X-ray diffraction
1.7Å resolution

Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V).

Released:
DOI: 10.2210/pdb1m16/pdb
PDB entry 1m16 coloured by chain, front view.
PDB entry 1m16 coloured by chain, side view.
PDB entry 1m16 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: 146 amino acids
Theoretical weight: 16.72 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 2 x SO4
Ligand FMT 2 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: C2221
Unit cell:
a: 74.18Å b: 97.013Å c: 108.871Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.22 0.249
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)