1EV2: FGF2

Crystal structure of FGF2 in complex with the extracellular ligand binding domain of fgf receptor 2 (FGFR2). Determined by X-ray diffraction at 2.2 Å resolution. Released 31 May 2000.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 8
Atoms: 10,101
Mol. weight: 159.39 kDa
Released: 31 May 2000

Explore 1EV2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1EV2 contains 35 α-helices and 140 β-strands across 8 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.

Chains A, B, C and D: 1 helix, 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
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	94-98	5	1
β-strand	104-108	5	1
β-strand	115	1	1
β-strand	118	1	2
β-strand	123	1	1
β-strand	124	1	2
α-helix	127-129	3
β-strand	139-143	5	1

Chain E: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	152-156	5	9
α-helix	159-162	4
β-strand	166-170	5	10
β-strand	175-178	4	11
β-strand	181-184	4	9
α-helix	186-187	2
β-strand	188-193	6	10
β-strand	196-197	2	10
α-helix	200-202	3
β-strand	208-210	3	11
α-helix	211-213	3
β-strand	215-218	4	11
α-helix	223-225	3
β-strand	227-235	9	10
β-strand	238-249	12	10
β-strand	257-258	2	12
β-strand	266	1	13
β-strand	274-277	4	14
β-strand	280-281	2	12
α-helix	285-286	2
β-strand	287-293	7	13
β-strand	309-314	6	13
β-strand	316	1	15
β-strand	319	1	15
β-strand	326-329	4	14
α-helix	334-336	3
β-strand	338-345	8	13
β-strand	350-357	8	13

Chain F: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	152-156	5	16
α-helix	159-162	4
β-strand	166-170	5	17
β-strand	175-178	4	18
β-strand	181-184	4	16
α-helix	186-187	2
β-strand	188-193	6	17
β-strand	196-197	2	17
α-helix	200-202	3
β-strand	208-210	3	18
α-helix	211-213	3
β-strand	215-218	4	18
α-helix	223-225	3
β-strand	227-235	9	17
β-strand	238-249	12	17
β-strand	257-258	2	19
β-strand	266-267	2	20
β-strand	274-277	4	21
β-strand	280-281	2	19
α-helix	285-286	2
β-strand	287-292	6	20
β-strand	310-314	5	20
β-strand	316	1	22
β-strand	319	1	22
β-strand	326-329	4	21
α-helix	334-336	3
β-strand	338-345	8	20
β-strand	350-358	9	20

Chain G: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	152-156	5	23
α-helix	159-162	4
β-strand	166-170	5	24
β-strand	175-178	4	25
β-strand	181-184	4	23
α-helix	186-187	2
β-strand	188-193	6	24
β-strand	196-197	2	24
α-helix	200-202	3
β-strand	208-210	3	25
α-helix	211-213	3
β-strand	215-218	4	25
α-helix	223-225	3
β-strand	227-235	9	24
β-strand	238-249	12	24
β-strand	257-258	2	26
α-helix	264-265	2
β-strand	266-269	4	27
β-strand	274-277	4	28
β-strand	280-281	2	26
α-helix	285-286	2
β-strand	287-293	7	27
β-strand	309-314	6	27
β-strand	316	1	29
β-strand	319	1	29
β-strand	326-329	4	28
α-helix	334-336	3
β-strand	338-345	8	27
β-strand	350-360	11	27

Chain H: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	152-156	5	30
α-helix	159-162	4
β-strand	166-170	5	31
β-strand	175-178	4	32
β-strand	181-184	4	30
α-helix	186-187	2
β-strand	188-193	6	31
β-strand	196-197	2	31
α-helix	200-202	3
β-strand	208-210	3	32
α-helix	211-213	3
β-strand	215-218	4	32
α-helix	223-225	3
β-strand	227-235	9	31
β-strand	238-249	12	31
β-strand	257-258	2	33
α-helix	264-265	2
β-strand	266-269	4	34
β-strand	274-277	4	35
β-strand	280-281	2	33
α-helix	285-286	2
β-strand	287-293	7	34
β-strand	309-314	6	34
β-strand	316	1	36
β-strand	319	1	36
β-strand	326-329	4	35
α-helix	334-336	3
β-strand	338-345	8	34
β-strand	350-360	11	34
α-helix	361-362	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (fibroblast growth factor 2)	A, B, C, D	protein	132	Homo sapiens	P09038 (AlphaFold model)
Protein (fibroblast growth factor receptor 2)	E, F, G, H	protein	220	Homo sapiens	P21802 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1EV2_1 PROTEIN (FIBROBLAST GROWTH FACTOR 2) (chains A, B, C, D)
GHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVSANRYL
AMKEDGRLLASKSVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQ
KAILFLPMSAKS

Sequence of entity 2 (E, F, G, H), FASTA

>1EV2_2 PROTEIN (FIBROBLAST GROWTH FACTOR RECEPTOR 2) (chains E, F, G, H)
NSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGG
YKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANA
STVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEV
LYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGRE

Primary citation

Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. Plotnikov, A.N., Hubbard, S.R., Schlessinger, J. et al. Cell (2000) 101:413-424. DOI 10.1016/S0092-8674(00)80851-X · 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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