2M49: Fibroblast growth factor 2

Structural Insights into Human S100B and Basic Fibroblast Growth Factor (FGF2) Interaction. Determined by solution NMR. Released 18 Dec 2013.

Method: Solution NMR
Organism: Homo sapiens
Chains: 4
Atoms: 3,512
Mol. weight: 50.04 kDa
Released: 18 Dec 2013

Explore 2M49 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2M49 contains 15 α-helices and 28 β-strands across 4 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: 3 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	53-59	7	1
β-strand	62-67	6	1
β-strand	72-76	5	1
β-strand	82-85	4	1
β-strand	93-98	6	1
β-strand	104-108	5	1
β-strand	115	1	1
β-strand	117-118	2	2
β-strand	123	1	1
β-strand	124-125	2	2
α-helix	126	1
α-helix	127-129	3
β-strand	139-143	5	1

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	2-18	17
α-helix	30-36	7
α-helix	52-56	5
α-helix	70-86	17

Chain C: 3 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
β-strand	53-59	7	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	94-98	5	3
β-strand	104-108	5	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
β-strand	139-143	5	3

Chain D: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	93-109	17
α-helix	121-129	9
α-helix	143-151	9
α-helix	161-176	16
α-helix	177-179	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibroblast growth factor 2	A, C	protein	126	Homo sapiens	P09038 (AlphaFold model)
Protein S100-B	B, D	protein	91	Homo sapiens	P04271 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2M49_1 Fibroblast growth factor 2 (chains A, C)
DPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVSANRYLAMKE
DGRLLASKSVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAIL
FLPMSA

Sequence of entity 2 (B, D), FASTA

>2M49_2 Protein S100-B (chains B, D)
SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETL
DNDGDGECDFQEFMAFVAMVTTACHEFFEHE

Primary citation

Structural insights into the interaction of human S100B and basic fibroblast growth factor (FGF2): Effects on FGFR1 receptor signaling. Gupta, A.A., Chou, R.H., Li, H. et al. Biochim Biophys Acta (2013) 1834:2606-2619. DOI 10.1016/j.bbapap.2013.09.012 · 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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