1IIL: PRO253ARG apert mutant fgf receptor 2

Crystal structure of PRO253ARG apert mutant fgf receptor 2 (FGFR2) in complex with FGF2. Determined by X-ray diffraction at 2.3 Å resolution. Released 9 May 2001.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 8
Atoms: 10,677
Mol. weight: 167.8 kDa
Released: 9 May 2001

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

Secondary structure: helices and β-sheets

1IIL contains 50 α-helices and 132 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 and B: 3 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	30-34	5	1
β-strand	39-43	5	1
β-strand	49-52	4	1
α-helix	58-60	3
β-strand	62-68	7	1
β-strand	71-76	6	1
β-strand	81-85	5	1
β-strand	91-94	4	1
β-strand	103-107	5	1
β-strand	113-117	5	1
β-strand	124	1	1
β-strand	127	1	2
β-strand	132	1	1
β-strand	133	1	2
α-helix	136-138	3
α-helix	144-146	3
β-strand	148-152	5	1

Chains C and D: 4 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	30-34	5	5
β-strand	39-43	5	5
β-strand	49-52	4	5
α-helix	58-60	3
β-strand	62-68	7	5
β-strand	71-76	6	5
β-strand	81-85	5	5
β-strand	91-94	4	5
α-helix	99-101	3
β-strand	103-107	5	5
β-strand	113-117	5	5
β-strand	124	1	5
β-strand	127	1	6
β-strand	132	1	5
β-strand	133	1	6
α-helix	136-138	3
α-helix	144-146	3
β-strand	148-152	5	5

Chains E, F, G and H: 9 helices, 19 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
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
α-helix	259	1
α-helix	264-265	2
β-strand	266-269	4	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
α-helix	321-323	3
β-strand	326-329	4	14
α-helix	334-336	3
β-strand	338-345	8	13
β-strand	350-360	11	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Heparin-binding growth factor 2	A, B, C, D	protein	155	Homo sapiens	P09038 (AlphaFold model)
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

>1IIL_1 HEPARIN-BINDING GROWTH FACTOR 2 (chains A, B, C, D)
MAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHI
KLQLQAEERGVVSIKGVSANRYLAMKEDGRLLASKSVTDECFFFERLESNNYNTYRSRKY
TSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS

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

>1IIL_2 FIBROBLAST GROWTH FACTOR RECEPTOR 2 (chains E, F, G, H)
NSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGG
YKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSRHRPILQAGLPANA
STVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEV
LYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGRE

Primary citation

Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome. Ibrahimi, O.A., Eliseenkova, A.V., Plotnikov, A.N. et al. Proc Natl Acad Sci U S A (2001) 98:7182-7187. DOI 10.1073/pnas.121183798 · 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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