1FGA: Basic fibroblast growth factor

Name: PDB 1FGA: Refinement of the structure of human basic fibroblast growth factor at 1.6 Å resolution and analysis of presumed heparin binding sites by selenate substitution
Published: 1993-07-15
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: growth factor

Refinement of the structure of human basic fibroblast growth factor at 1.6 Å resolution and analysis of presumed heparin binding sites by selenate substitution. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Jul 1993.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,085
Mol. weight: 16.88 kDa
Ligands: SE4
Released: 15 Jul 1993

Explore 1FGA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FGA contains 3 α-helices and 15 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	22-25	4	1
β-strand	31-34	4	1
β-strand	40-43	4	1
α-helix	49-51	3
β-strand	53-59	7	2
β-strand	62-67	6	2
β-strand	73-76	4	2
β-strand	82-85	4	2
β-strand	94-95	2	2
β-strand	98	1	1
β-strand	104	1	1
β-strand	107-108	2	2
β-strand	115	1	2
β-strand	118	1	3
β-strand	124	1	3
α-helix	127-129	3
α-helix	135-137	3
β-strand	139-142	4	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Basic fibroblast growth factor	A	protein	146	Homo sapiens	P09038 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1FGA_1 BASIC FIBROBLAST GROWTH FACTOR (chains A)
PALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEER
GVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKR
TGQYKLGSKTGPGQKAILFLPMSAKS

Ligands and cofactors

ID	Name	Formula	Copies
SE4	Selenate ion	O4 Se	2

Water and common crystallization additives (BME) are not listed.

Primary citation

Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution. Eriksson, A.E., Cousens, L.S., Matthews, B.W. Protein Sci (1993) 2:1274-1284. PubMed

Other PDB entries of the same protein (UniProt P09038 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8OM6 1.31 Å, Crystal structure of FGF2-STAB, a stable variant of human fibroblast growth factor 2
8HU7 1.4 Å, Crystal structure of FGF2-M1 mutant - D28E/C78L/C96I/S137P
8HUE 1.48 Å, Crystal structure of FGF2-M2 mutant - D28E/C78I/C96I/S137P
4OEE 1.5 Å, Crystal Structure Analysis of FGF2-Disaccharide (S3I2) complex
1BFG 1.6 Å, Crystal structure of basic fibroblast growth factor at 1.6 Å resolution
4FGF 1.6 Å, Refinement of the structure of human basic fibroblast growth factor at 1.6 Å resolution…
4OEG 1.6 Å, Crystal Structure Analysis of FGF2-Disaccharide (S9I2) complex
2FGF 1.77 Å, Three-dimensional structure of human basic fibroblast growth factor, A structural…
4OEF 1.8 Å, Crystal Structure Analysis of FGF2-Disaccharide (S6I2) complex
1BAS 1.9 Å, Three-dimensional structures of acidic and basic fibroblast growth factors
1BFB 1.9 Å, Basic fibroblast growth factor complexed with heparin tetramer fragment
5X1O 1.9 Å, PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface…

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