5X1O: Fibroblast growth factor 2

PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface to facilitate the unconventional oligomerization-dependent secretion process as revealed by a combined FTIR/NMR/X-ray study. Determined by X-ray diffraction at 1.9 Å resolution. Released 7 Mar 2018.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,291
Mol. weight: 33.71 kDa
Ligands: I3P
Released: 7 Mar 2018

Explore 5X1O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5X1O contains 11 α-helices and 28 β-strands across 2 chains. 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: 6 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	21-25	5	1
β-strand	30-34	5	1
β-strand	40-43	4	1
α-helix	49-51	3
β-strand	53-57	5	1
β-strand	62-67	6	1
β-strand	72-76	5	1
β-strand	82-85	4	1
α-helix	90-92	3
β-strand	94-99	6	1
α-helix	100-102	3
β-strand	103-108	6	1
β-strand	115	1	1
β-strand	118	1	2
β-strand	123	1	1
β-strand	124	1	2
α-helix	125-126	2
α-helix	127-129	3
α-helix	135-137	3
β-strand	139-142	4	1

Chain B: 5 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	21-25	5	3
β-strand	30-34	5	3
β-strand	40-43	4	3
α-helix	49-51	3
β-strand	53-57	5	3
β-strand	62-67	6	3
β-strand	72-76	5	3
β-strand	82-85	4	3
α-helix	90-92	3
β-strand	94-99	6	3
β-strand	103-108	6	3
β-strand	115	1	3
β-strand	118	1	4
β-strand	123	1	3
β-strand	124	1	4
α-helix	125-126	2
α-helix	127-129	3
α-helix	135-137	3
β-strand	139-142	4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibroblast growth factor 2	A, B	protein	146	Homo sapiens	P09038 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5X1O_1 Fibroblast growth factor 2 (chains A, B)
PALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEER
GVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKR
TGQYKLGSKTGPGQKAILFLPMSAKS

Ligands and cofactors

ID	Name	Formula	Copies
I3P	D-myo-inositol-1,4,5-triphosphate	C6 H15 O15 P3	2

Primary citation

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
1BFF 2.0 Å, The 154 amino acid form of human basic fibroblast growth factor

Browse structure collections

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