PDBsum entry 3cqa

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Hormone PDB id
Protein chains
140 a.a. *
SO4 ×2
FMT ×2
Waters ×220
* Residue conservation analysis
PDB id:
Name: Hormone
Title: Crystal structure of human fibroblast growth factor-1 with mutations glu81ala and lys101ala
Structure: Heparin-binding growth factor 1. Chain: a, b. Fragment: unp residues 16-152. Synonym: hbgf-1, acidic fibroblast growth factor, afgf, beta-endothelial cell growth factor, ecgf- beta. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Gene: fgf1, fgfa. Expressed in: escherichia coli.
1.80Å     R-factor:   0.191     R-free:   0.212
Authors: A.K.Meher,E.Honjo,R.Kuroki,J.Lee,T.Somasundaram,M.Blaber
Key ref: A.K.Meher et al. (2009). Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 1136-1140. PubMed id: 19923735
02-Apr-08     Release date:   07-Apr-09    
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Protein chains
Pfam   ArchSchema ?
P05230  (FGF1_HUMAN) -  Fibroblast growth factor 1
155 a.a.
140 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   9 terms 
  Biological process     Fc-epsilon receptor signaling pathway   29 terms 
  Biochemical function     S100 protein binding     7 terms  


Acta Crystallogr Sect F Struct Biol Cryst Commun 65:1136-1140 (2009)
PubMed id: 19923735  
Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.
A.K.Meher, S.I.Blaber, J.Lee, E.Honjo, R.Kuroki, M.Blaber.
Large-volume protein crystals are a prerequisite for neutron diffraction studies and their production represents a bottleneck in obtaining neutron structures. Many protein crystals that permit the collection of high-resolution X-ray diffraction data are inappropriate for neutron diffraction owing to a plate-type morphology that limits the crystal volume. Human fibroblast growth factor 1 crystallizes in a plate morphology that yields atomic resolution X-ray diffraction data but has insufficient volume for neutron diffraction. The thin physical dimension has been identified as corresponding to the b cell edge and the X-ray structure identified a solvent-mediated crystal contact adjacent to position Glu81 that was hypothesized to limit efficient crystal growth in this dimension. In this report, a series of mutations at this crystal contact designed to both reduce side-chain entropy and replace the solvent-mediated interface with direct side-chain contacts are reported. The results suggest that improved crystal growth is achieved upon the introduction of direct crystal contacts, while little improvement is observed with side-chain entropy-reducing mutations alone.