1CJF: Protein

Profilin binds proline-rich ligands in two distinct amide backbone orientations. Determined by X-ray diffraction at 2.3 Å resolution. Released 7 Jul 1999.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,343
Mol. weight: 33.27 kDa
Ligands: HOM
Released: 7 Jul 1999

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

Secondary structure: helices and β-sheets

1CJF contains 16 α-helices and 14 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: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	5-11	7
β-strand	16-23	8	1
β-strand	29-33	5	1
α-helix	39-41	3
α-helix	44-51	8
α-helix	58-61	4
β-strand	63-65	3	1
β-strand	68-76	9	1
β-strand	84-89	6	1
α-helix	95-97	3
β-strand	99-104	6	1
β-strand	108-114	7	1
α-helix	115	1
α-helix	120-136	17

Chain B: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	4-11	8
β-strand	16-23	8	2
β-strand	29-33	5	2
α-helix	39-41	3
α-helix	44-51	8
α-helix	58-61	4
β-strand	63-65	3	2
β-strand	68-75	8	2
β-strand	84-89	6	2
α-helix	95-97	3
β-strand	99-104	6	2
β-strand	108-114	7	2
α-helix	115	1
α-helix	120-135	16

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-15	13

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (human platelet profilin)	A, B	protein	139	Homo sapiens	P07737 (AlphaFold model)
Protein (proline peptide)	C, D	protein	15

Sequence of entity 1 (A, B), FASTA

>1CJF_1 PROTEIN (HUMAN PLATELET PROFILIN) (chains A, B)
AGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYV
NGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHG
GLINKKCYEMASHLRRSQY

Sequence of entity 2 (C, D), FASTA

>1CJF_2 PROTEIN (PROLINE PEPTIDE) (chains C, D)
PPPPPPPPPPPPPPP

Ligands and cofactors

ID	Name	Formula	Copies
HOM	7-hydroxy-4-methyl-3-(2-hydroxy-ethyl)coumarin	C12 H12 O4	2

Primary citation

Profilin binds proline-rich ligands in two distinct amide backbone orientations. Mahoney, N.M., Rozwarski, D.A., Fedorov, E. et al. Nat Struct Biol (1999) 6:666-671. DOI 10.1038/10722 · PubMed

Other PDB entries of the same protein (UniProt P07737 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
8BJH 1.69 Å, chimera of the inactive ExoY Nucleotidyl Cyclase domain from Vibrio nigripulchritudo…
8BJJ 1.7 Å, ExoY Nucleotidyl Cyclase domain from Vibrio nigripulchritudo MARTX toxin, bound to…
8BJI 1.75 Å, chimera of ExoY Nucleotidyl Cyclase domain from Vibrio nigripulchritudo fused to a…
2PAV 1.8 Å, Ternary complex of Profilin-Actin with the Last Poly-Pro of Human VASP
1FIL 2.0 Å, Human platelet profilin I crystallized in high salt actin-binding protein
6NBE 2.0 Å, Ternary Complex of Ac-Alpha-Actin with Profilin and CoA-NAA80
4X1L 2.16 Å, Structural basis for mutation-induced destabilization of Profilin 1 in ALS
4X1M 2.17 Å, Structural basis for mutation-induced destabilization of Profilin 1 in ALS
1AWI 2.2 Å, Human platelet profilin complexed with the L-PRO10 peptide
1CF0 2.2 Å, Human platelet profilin complexed with an L-PRO10-iodotyrosine peptide
8BR0 2.22 Å, ExoY Nucleotidyl Cyclase domain from Vibrio nigripulchritudo MARTX toxin (residue Q3455…

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